Chemical groups containing the covalent disulfide bonds -S-S-. The sulfur atoms can be bound to inorganic or organic moieties.
Compounds containing the -SH radical.
A family of thioltransferases that contain two active site CYSTEINE residues, which either form a disulfide (oxidized form) or a dithiol (reduced form). They function as an electron carrier in the GLUTHIONE-dependent synthesis of deoxyribonucleotides by RIBONUCLEOTIDE REDUCTASES and may play a role in the deglutathionylation of protein thiols. The oxidized forms of glutaredoxins are directly reduced by the GLUTATHIONE.
A GLUTATHIONE dimer formed by a disulfide bond between the cysteine sulfhydryl side chains during the course of being oxidized.
A thiol-containing non-essential amino acid that is oxidized to form CYSTINE.
A reagent commonly used in biochemical studies as a protective agent to prevent the oxidation of SH (thiol) groups and for reducing disulphides to dithiols.
Sulfur-sulfur bond isomerases that catalyze the rearrangement of disulfide bonds within proteins during folding. Specific protein disulfide-isomerase isoenzymes also occur as subunits of PROCOLLAGEN-PROLINE DIOXYGENASE.
A radiation-protective agent that interferes with sulfhydryl enzymes. It may also protect against carbon tetrachloride liver damage.
A chemical reaction in which an electron is transferred from one molecule to another. The electron-donating molecule is the reducing agent or reductant; the electron-accepting molecule is the oxidizing agent or oxidant. Reducing and oxidizing agents function as conjugate reductant-oxidant pairs or redox pairs (Lehninger, Principles of Biochemistry, 1982, p471).
A covalently linked dimeric nonessential amino acid formed by the oxidation of CYSTEINE. Two molecules of cysteine are joined together by a disulfide bridge to form cystine.
A tripeptide with many roles in cells. It conjugates to drugs to make them more soluble for excretion, is a cofactor for some enzymes, is involved in protein disulfide bond rearrangement and reduces peroxides.
Hydrogen-donating proteins that participates in a variety of biochemical reactions including ribonucleotide reduction and reduction of PEROXIREDOXINS. Thioredoxin is oxidized from a dithiol to a disulfide when acting as a reducing cofactor. The disulfide form is then reduced by NADPH in a reaction catalyzed by THIOREDOXIN REDUCTASE.
A standard reagent for the determination of reactive sulfhydryl groups by absorbance measurements. It is used primarily for the determination of sulfhydryl and disulfide groups in proteins. The color produced is due to the formation of a thio anion, 3-carboxyl-4-nitrothiophenolate.
An enzyme that catalyzes the reduction of a protein-disulfide in the presence of glutathione, forming a protein-dithiol. Insulin is one of its substrates. EC 1.8.4.2.
An alkylating sulfhydryl reagent. Its actions are similar to those of iodoacetate.
Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.
A sulfhydryl reagent which oxidizes sulfhydryl groups to the disulfide form. It is a radiation-sensitizing agent of anoxic bacterial and mammalian cells.
The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9)
A class of organic compounds which contain two rings that share a pair of bridgehead carbon atoms.
Oxidoreductases with specificity for oxidation or reduction of SULFUR COMPOUNDS.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
A compound that, along with its isomer, Cleland's reagent (DITHIOTHREITOL), is used for the protection of sulfhydryl groups against oxidation to disulfides and for the reduction of disulfides to sulfhydryl groups.
Cell surface proteins that bind amino acids and trigger changes which influence the behavior of cells. Glutamate receptors are the most common receptors for fast excitatory synaptic transmission in the vertebrate central nervous system, and GAMMA-AMINOBUTYRIC ACID and glycine receptors are the most common receptors for fast inhibition.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
A class of enzymes that catalyze geometric or structural changes within a molecule to form a single product. The reactions do not involve a net change in the concentrations of compounds other than the substrate and the product.(from Dorland, 28th ed) EC 5.
Chemical groups containing the covalent sulfur bonds -S-. The sulfur atom can be bound to inorganic or organic moieties.
The rate dynamics in chemical or physical systems.
A FLAVOPROTEIN enzyme that catalyzes the oxidation of THIOREDOXINS to thioredoxin disulfide in the presence of NADP+. It was formerly listed as EC 1.6.4.5
Chemical agents that react with SH groups. This is a chemically diverse group that is used for a variety of purposes. Among these are enzyme inhibition, enzyme reactivation or protection, and labelling.
Iodinated derivatives of acetic acid. Iodoacetates are commonly used as alkylating sulfhydryl reagents and enzyme inhibitors in biochemical research.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
A derivative of ACETIC ACID that contains one IODINE atom attached to its methyl group.
Benzoic acid esters or salts substituted with one or more iodine atoms.
The covalent bonding of an alkyl group to an organic compound. It can occur by a simple addition reaction or by substitution of another functional group.
A sulfhydryl reagent that is widely used in experimental biochemical studies.
A glycoprotein albumin from hen's egg white with strong iron-binding affinity.
Any of the monobasic inorganic or organic acids of sulfur with the general formula RSO(OH). (From McGraw Hill Dictionary of Scientific and Technical Terms, 4th ed)
Liquid chromatographic techniques which feature high inlet pressures, high sensitivity, and high speed.
Inorganic or organic compounds derived from phosphine (PH3) by the replacement of H atoms. (From Grant & Hackh's Chemical Dictionary, 5th ed)
An enzyme that catalyzes the endonucleolytic cleavage of pancreatic ribonucleic acids to 3'-phosphomono- and oligonucleotides ending in cytidylic or uridylic acids with 2',3'-cyclic phosphate intermediates. EC 3.1.27.5.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
An intermediate in the pathway of coenzyme A formation in mammalian liver and some microorganisms.
A basic aluminum complex of sulfated sucrose.
Toxins, contained in cobra (Naja) venom that block cholinergic receptors; two specific proteins have been described, the small (short, Type I) and the large (long, Type II) which also exist in other Elapid venoms.
Materials that add an electron to an element or compound, that is, decrease the positiveness of its valence. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
The maturing process of SPERMATOZOA after leaving the testicular SEMINIFEROUS TUBULES. Maturation in SPERM MOTILITY and FERTILITY takes place in the EPIDIDYMIS as the sperm migrate from caput epididymis to cauda epididymis.
Procedures by which protein structure and function are changed or created in vitro by altering existing or synthesizing new structural genes that direct the synthesis of proteins with sought-after properties. Such procedures may include the design of MOLECULAR MODELS of proteins using COMPUTER GRAPHICS or other molecular modeling techniques; site-specific mutagenesis (MUTAGENESIS, SITE-SPECIFIC) of existing genes; and DIRECTED MOLECULAR EVOLUTION techniques to create new genes.
A species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
Proteins prepared by recombinant DNA technology.
Disruption of the non-covalent bonds and/or disulfide bonds responsible for maintaining the three-dimensional shape and activity of the native protein.
An analytical method used in determining the identity of a chemical based on its mass using mass analyzers/mass spectrometers.
Carrier proteins for OXYTOCIN and VASOPRESSIN. They are polypeptides of about 10-kDa, synthesized in the HYPOTHALAMUS. Neurophysin I is associated with oxytocin and neurophysin II is associated with vasopressin in their respective precursors and during transportation down the axons to the neurohypophysis (PITUITARY GLAND, POSTERIOR).
Rhodium. A hard and rare metal of the platinum group, atomic number 45, atomic weight 102.905, symbol Rh. (Dorland, 28th ed)
The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.
A group of organic sulfur-containing nitrites, alkyl thionitrites. S-Nitrosothiols include compounds such as S-NITROSO-N-ACETYLPENICILLAMINE and S-NITROSOGLUTATHIONE.
Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
A highly caustic substance that is used to neutralize acids and make sodium salts. (From Merck Index, 11th ed)
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.
The location of the atoms, groups or ions relative to one another in a molecule, as well as the number, type and location of covalent bonds.
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
Analysis of PEPTIDES that are generated from the digestion or fragmentation of a protein or mixture of PROTEINS, by ELECTROPHORESIS; CHROMATOGRAPHY; or MASS SPECTROMETRY. The resulting peptide fingerprints are analyzed for a variety of purposes including the identification of the proteins in a sample, GENETIC POLYMORPHISMS, patterns of gene expression, and patterns diagnostic for diseases.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
Catalyzes the oxidation of GLUTATHIONE to GLUTATHIONE DISULFIDE in the presence of NADP+. Deficiency in the enzyme is associated with HEMOLYTIC ANEMIA. Formerly listed as EC 1.6.4.2.
A single-chain polypeptide derived from bovine tissues consisting of 58 amino-acid residues. It is an inhibitor of proteolytic enzymes including CHYMOTRYPSIN; KALLIKREIN; PLASMIN; and TRYPSIN. It is used in the treatment of HEMORRHAGE associated with raised plasma concentrations of plasmin. It is also used to reduce blood loss and transfusion requirements in patients at high risk of major blood loss during and following open heart surgery with EXTRACORPOREAL CIRCULATION. (Reynolds JEF(Ed): Martindale: The Extra Pharmacopoeia (electronic version). Micromedex, Inc, Englewood, CO, 1995)
The parts of a macromolecule that directly participate in its specific combination with another molecule.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
Serine proteinase inhibitors which inhibit trypsin. They may be endogenous or exogenous compounds.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
A group of oxidoreductases that act on NADH or NADPH. In general, enzymes using NADH or NADPH to reduce a substrate are classified according to the reverse reaction, in which NAD+ or NADP+ is formally regarded as an acceptor. This subclass includes only those enzymes in which some other redox carrier is the acceptor. (Enzyme Nomenclature, 1992, p100) EC 1.6.
The process by which two molecules of the same chemical composition form a condensation product or polymer.
Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
Reagents with two reactive groups, usually at opposite ends of the molecule, that are capable of reacting with and thereby forming bridges between side chains of amino acids in proteins; the locations of naturally reactive areas within proteins can thereby be identified; may also be used for other macromolecules, like glycoproteins, nucleic acids, or other.
A strong oxidizing agent used in aqueous solution as a ripening agent, bleach, and topical anti-infective. It is relatively unstable and solutions deteriorate over time unless stabilized by the addition of acetanilide or similar organic materials.
A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.
A family of cellular proteins that mediate the correct assembly or disassembly of polypeptides and their associated ligands. Although they take part in the assembly process, molecular chaperones are not components of the final structures.
Theoretical representations that simulate the behavior or activity of chemical processes or phenomena; includes the use of mathematical equations, computers, and other electronic equipment.
A strong corrosive acid that is commonly used as a laboratory reagent. It is formed by dissolving hydrogen chloride in water. GASTRIC ACID is the hydrochloric acid component of GASTRIC JUICE.
The phenomenon whereby certain chemical compounds have structures that are different although the compounds possess the same elemental composition. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 5th ed)
A family of ubiquitously-expressed peroxidases that play a role in the reduction of a broad spectrum of PEROXIDES like HYDROGEN PEROXIDE; LIPID PEROXIDES and peroxinitrite. They are found in a wide range of organisms, such as BACTERIA; PLANTS; and MAMMALS. The enzyme requires the presence of a thiol-containing intermediate such as THIOREDOXIN as a reducing cofactor.
A strong organic base existing primarily as guanidium ions at physiological pH. It is found in the urine as a normal product of protein metabolism. It is also used in laboratory research as a protein denaturant. (From Martindale, the Extra Pharmacopoeia, 30th ed and Merck Index, 12th ed) It is also used in the treatment of myasthenia and as a fluorescent probe in HPLC.
A system of cisternae in the CYTOPLASM of many cells. In places the endoplasmic reticulum is continuous with the plasma membrane (CELL MEMBRANE) or outer membrane of the nuclear envelope. If the outer surfaces of the endoplasmic reticulum membranes are coated with ribosomes, the endoplasmic reticulum is said to be rough-surfaced (ENDOPLASMIC RETICULUM, ROUGH); otherwise it is said to be smooth-surfaced (ENDOPLASMIC RETICULUM, SMOOTH). (King & Stansfield, A Dictionary of Genetics, 4th ed)
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
The naturally occurring or experimentally induced replacement of one or more AMINO ACIDS in a protein with another. If a functionally equivalent amino acid is substituted, the protein may retain wild-type activity. Substitution may also diminish, enhance, or eliminate protein function. Experimentally induced substitution is often used to study enzyme activities and binding site properties.
The sum of the weight of all the atoms in a molecule.
Nicotinamide adenine dinucleotide phosphate. A coenzyme composed of ribosylnicotinamide 5'-phosphate (NMN) coupled by pyrophosphate linkage to the 5'-phosphate adenosine 2',5'-bisphosphate. It serves as an electron carrier in a number of reactions, being alternately oxidized (NADP+) and reduced (NADPH). (Dorland, 27th ed)
A change from planar to elliptic polarization when an initially plane-polarized light wave traverses an optically active medium. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
An enzyme that catalyzes the conversion of (S)-malate and NAD+ to oxaloacetate and NADH. EC 1.1.1.37.
The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.
A basic enzyme that is present in saliva, tears, egg white, and many animal fluids. It functions as an antibacterial agent. The enzyme catalyzes the hydrolysis of 1,4-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrin. EC 3.2.1.17.
A representation, generally small in scale, to show the structure, construction, or appearance of something. (From Random House Unabridged Dictionary, 2d ed)
Pathological processes involving the STOMACH.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
A disturbance in the prooxidant-antioxidant balance in favor of the former, leading to potential damage. Indicators of oxidative stress include damaged DNA bases, protein oxidation products, and lipid peroxidation products (Sies, Oxidative Stress, 1991, pxv-xvi).
An element with atomic symbol O, atomic number 8, and atomic weight [15.99903; 15.99977]. It is the most abundant element on earth and essential for respiration.

The disulfide-bonded loop of chromogranin B mediates membrane binding and directs sorting from the trans-Golgi network to secretory granules. (1/5505)

The disulfide-bonded loop of chromogranin B (CgB), a regulated secretory protein with widespread distribution in neuroendocrine cells, is known to be essential for the sorting of CgB from the trans-Golgi network (TGN) to immature secretory granules. Here we show that this loop, when fused to the constitutively secreted protein alpha1-antitrypsin (AT), is sufficient to direct the fusion protein to secretory granules. Importantly, the sorting efficiency of the AT reporter protein bearing two loops (E2/3-AT-E2/3) is much higher compared with that of AT with a single disulfide-bonded loop. In contrast to endogenous CgB, E2/3-AT-E2/3 does not undergo Ca2+/pH-dependent aggregation in the TGN. Furthermore, the disulfide-bonded loop of CgB mediates membrane binding in the TGN and does so with 5-fold higher efficiency if two loops are present on the reporter protein. The latter finding supports the concept that under physiological conditions, aggregates of CgB are the sorted units of cargo which have multiple loops on their surface leading to high membrane binding and sorting efficiency of CgB in the TGN.  (+info)

Chaperone activity with a redox switch. (2/5505)

Hsp33, a member of a newly discovered heat shock protein family, was found to be a very potent molecular chaperone. Hsp33 is distinguished from all other known molecular chaperones by its mode of functional regulation. Its activity is redox regulated. Hsp33 is a cytoplasmically localized protein with highly reactive cysteines that respond quickly to changes in the redox environment. Oxidizing conditions like H2O2 cause disulfide bonds to form in Hsp33, a process that leads to the activation of its chaperone function. In vitro and in vivo experiments suggest that Hsp33 protects cells from oxidants, leading us to conclude that we have found a protein family that plays an important role in the bacterial defense system toward oxidative stress.  (+info)

Insulin-like growth factors I and II are unable to form and maintain their native disulfides under in vivo redox conditions. (3/5505)

Insulin-like growth factor (IGF) I does not quantitatively form its three native disulfide bonds in the presence of 10 mM reduced and 1 mM oxidized glutathione in vitro [Hober, S. et al. (1992) Biochemistry 31, 1749-1756]. In this paper, we show (i) that both IGF-I and IGF-II are unable to form and maintain their native disulfide bonds at redox conditions that are similar to the situation in the secretory vesicles in vivo and (ii) that the presence of protein disulfide isomerase does not overcome this problem. The results indicate that the previously described thermodynamic disulfide exchange folding problem of IGF-I in vitro is also present in vivo. Speculatively, we suggest that the thermodynamic disulfide exchange properties of IGF-I and II are biologically significant for inactivation of the unbound growth factors by disulfide exchange reactions to generate variants destined for rapid clearance.  (+info)

In vivo formation of Cu,Zn superoxide dismutase disulfide bond in Escherichia coli. (4/5505)

We have found that the in vivo folding of periplasmic Escherichia coli Cu,Zn superoxide dismutase is assisted by DsbA, which catalyzes the efficient formation of its single disulfide bond, whose integrity is essential to ensure full catalytic activity to the enzyme. In line with these findings, we also report that the production of recombinant Xenopus laevis Cu,Zn superoxide dismutase is enhanced when the enzyme is exported in the periplasmic space or is expressed in thioredoxin reductase mutant strains. Our data show that inefficient disulfide bond oxidation in the bacterial cytoplasm inhibits Cu,Zn superoxide dismutase folding in this cellular compartment.  (+info)

Scrotal heat stress induces altered sperm chromatin structure associated with a decrease in protamine disulfide bonding in the stallion. (5/5505)

A variety of testicular insults can induce changes in the structure of spermatozoal chromatin, resulting in spermatozoal DNA that is more susceptible to acid-induced denaturation. The degree of change in the DNA can be measured using the sperm chromatin structure assay (SCSA). The SCSA measures the relative amounts of single- and double-stranded DNA after staining with the metachromatic dye, acridine orange. Here we used a stallion model (n = 4) to study the effects of scrotal heat stress on spermatozoal DNA. This model was created by insulating stallion testes for 48 h and collecting sperm daily thereafter for 60 days. Changes in the SCSA were then correlated with protamine disulfide content and protamine types and levels. Results of the SCSA indicated that the susceptibility of spermatozoal DNA to denaturation was dependent on the spermatogenic cell stage that the ejaculated sperm was in at the time of the heat stress. Spermatozoa with altered DNA had a decrease in the extent of disulfide bonding that was associated with an increase in the susceptibility of DNA to denaturation. However, there were no detectable changes in either the protamine type or level. Thus, in this model, decreased disulfide bonding is associated with an increased susceptibility of spermatozoal DNA to denaturation in the absence of protamine changes.  (+info)

An intact sperm nuclear matrix may be necessary for the mouse paternal genome to participate in embryonic development. (6/5505)

We have been interested in determining the minimally required elements in the sperm head that are necessary in order for the paternal genome to participate in embryogenesis. We used an ionic detergent, mixed alkyltrimethylammonium bromide (ATAB), plus dithiothreitol (DTT) to remove the acrosome and almost all of the perinuclear theca, leaving only the sperm nucleus morphologically intact. We also tested the stability of the sperm nuclear matrix by the ability to form nuclear halos. Sperm nuclei washed in freshly prepared 0.5% ATAB + 2 mM DTT completely decondensed when extracted with salt, but nuclei washed in the same buffer that was 1 wk old, and then extracted with salt, produced nuclear halos, indicating stable nuclear matrices. When we treated sperm heads with freshly prepared ATAB+DTT and injected them into oocytes, none of the oocytes developed into live offspring. In contrast, sperm heads treated in the same way but with 1-wk-old ATAB+DTT solution could support development of about 30% of the oocytes to live offspring. Electron microscopy demonstrated that most of the perinuclear theca had been removed in both cases. These data suggest that at least in the mouse, the only component of the spermatozoa that is crucial for participation in embryologic development is the sperm nucleus with a stable nuclear matrix.  (+info)

The internal Cys-207 of sorghum leaf NADP-malate dehydrogenase can form mixed disulphides with thioredoxin. (7/5505)

The role of the internal Cys-207 of sorghum NADP-malate dehydrogenase (NADP-MDH) in the activation of the enzyme has been investigated through the examination of the ability of this residue to form mixed disulphides with thioredoxin mutated at either of its two active-site cysteines. The h-type Chlamydomonas thioredoxin was used, because it has no additional cysteines in the primary sequence besides the active-site cysteines. Both thioredoxin mutants proved equally efficient in forming mixed disulphides with an NADP-MDH devoid of its N-terminal bridge either by truncation, or by mutation of its N-terminal cysteines. They were poorly efficient with the more compact WT oxidised NADP-MDH. Upon mutation of Cys-207, no mixed disulphide could be formed, showing that this cysteine is the only one, among the four internal cysteines, which can form mixed disulphides with thioredoxin. These experiments confirm that the opening of the N-terminal disulphide loosens the interaction between subunits, making Cys-207, located at the dimer contact area, more accessible.  (+info)

Hairpin-shaped DNA duplexes with disulfide bonds in sugar-phosphate backbone as potential DNA reagents for crosslinking with proteins. (8/5505)

Convenient approaches were described to incorporate -OP(=O)O(-)-SS-O(-)(O=)PO- bridges in hairpin-shaped DNA duplexes instead of regular phosphodiester linkages: (i) H2O2- or 2,2'-dipyridyldisulfide-mediated coupling of 3'- and 5'-thiophosphorylated oligonucleotides on complementary template and (ii) more selective template-guided autoligation of a preactivated oligonucleotide derivative with an oligomer carrying a terminal thiophosphoryl group. Dithiothreitol was found to cleave completely modified internucleotide linkage releasing starting oligonucleotides. The presence of complementary template as an intrinsic element of the molecule protects the hairpin DNA analog from spontaneous exchange of disulfide-linked oligomer fragments and makes it a good candidate for auto-crosslinking with cysteine-containing proteins.  (+info)

Rabbit light chain 3315, prepared from a homogeneous antipneumococcal antibody, was subjected to hydrolysis by pepsin without prior reduction and alkylation of the intrachain disulfide bonds. Gel filtration of the hydrolysate on Sephadex G-10, G-15, and G-25 and ion exchange chromatography on SP-Sephadex yielded several disulfide bridge peptides. These were fully reduced and alkylated and sequenced by Edman degradation. The peptides were located in the light chain sequence determined in independent studies from our laboratory.. The half-cystine residues in this κB rabbit chain are located at positions 23, 80, 88, 134, 171, 194, and 214. The extra disulfide bridge extends between residues 80 and 171, thus joining the variable and constant domains. This is consistent with x-ray diffraction crystallographic studies showing that the corresponding residues in human light chains are separated by a distance compatible with disulfide bond formation.. ...
The integrity of antibody structure, stability, and biophysical characterization are becoming increasingly important as antibodies receive increasing scrutiny from regulatory authorities. We altered the disulfide bond arrangement of an IgG4 molecule by mutation of the Cys at the N terminus of the heavy chain constant domain 1 (CH1) (Kabat position 127) to a Ser and introduction of a Cys at a variety of positions (positions 227-230) at the C terminus of CH1. An inter-LC-CH1 disulfide bond is thus formed, which mimics the disulfide bond arrangement found in an IgG1 molecule. The antibody species present in the supernatant following transient expression in Chinese hamster ovary cells were analyzed by immunoblot to investigate product homogeneity, and purified product was analyzed by a thermofluor assay to determine thermal stability. We show that the light chain can form an inter-LC-CH1 disulfide bond with a Cys when present at several positions on the upper hinge (positions 227-230) and that such ...
Thiolates, not thiols, attack disulfide bonds. Hence, thiol-disulfide exchange is inhibited at low pH (typically, below 8) where the protonated thiol form is favored relative to the deprotonated thiolate form. (The pKa of a typical thiol group is roughly 8.3, but can vary due to its environment.) Thiol-disulfide exchange is the principal reaction by which disulfide bonds are formed and rearranged in a protein. The rearrangement of disulfide bonds within a protein generally occurs via intra-protein thiol-disulfide exchange reactions; a thiolate group of a cysteine residue attacks one of the proteins own disulfide bonds. This process of disulfide rearrangement (known as disulfide shuffling) does not change the number of disulfide bonds within a protein, merely their location (i.e., which cysteines are bonded). Disulfide reshuffling is generally much faster than oxidation/reduction reactions, which change the number of disulfide bonds within a protein. The oxidation and reduction of protein ...
Correct folding and disulfide bond formation is essential for the function of many secreted proteins including bacterial toxins, and their formation is facilitated by d is ulfide b ond forming (Dsb) oxidoreductase proteins, which usually contain a conserved thioredoxin (TRX) fold [1]. Protein disulfide bonds can serve structural roles, and thus are often buried in the core of a protein. However, in the case of Dsb proteins, partially exposed disulfide bonds in the TRX-fold CXXC motif have catalytic roles in protein folding, electron transport and bioenergetics in a variety of organisms [2, 3].. The Dsb proteins of Escherichia coli are the best characterized, and reside in its periplasm to correctly fold disulfide bond containing secreted and cell-wall proteins [4]. E. coli DsbA (Ec-DsbA) catalyzes the oxidation of disulfide bonds in reduced, unfolded proteins [5, 6], and is then re-oxidized by ubiquinone via E. coli DsbB (Ec-DsbB), an inner membrane transmembrane protein, which in turn is ...
Disulfide bonds play an important role in the folding and stability of many proteins.1-4 For example, S-S bonds are formed following the oxidative folding process between the thiol groups of cysteine, which can also hold different subunits of larger protein complexes together such as antibodies.5 These are also found in keratin in hair.6 In the refining of crude oil, oxidative desulfurization (ODS) of thiols forms the corresponding disulfides7 which then undergo further oxidation to thiosulfinates, disulfoxides, sulfinyl sulfones or disulfones. Disulfides are also used as vulcanizing agents for rubber8 and elastomers,9 in drugs,10 and in the design of rechargeable lithium batteries,11 for example. Traditionally, disulfides are produced through the oxidation of thiols in the presence of homogeneous catalysts including tributylammonium chlorochromate,12 metal phthalocyanines,13 cobalt(II) phthalocyanine tetrasodium sulfonate attached to poly(vinylamine),14 porphyrazinatocobalt(II) complex15 and ...
Protein folding, associated with isomerization of disulfide bonds, was studied using the mixed disulfide between glutathione and reduced ribonuclease T-1 (GS-RNase T-1) as a stable soluble and homogenous starting material; conditions were selected to model those within the lumen of the endoplasmic reticulum where native disulfide bonds are formed in protein biosynthesis, Folding was initiated by addition of free glutathione (GSH +/- GSSG) to promote thiol-disulfide interchange and was monitored by intrinsic protein fluorescence, appearance of native ribonuclease activity, HPLC, and nonreducing SDS-PAGE, All the analyses indicated that native RNase T-1 was recovered in high yield in a variety of redox conditions, Appearance of native activity followed first-order kinetics; kinetic analysis of the intrinsic fluorescence changes indicated an additional rapid process in some conditions, interpreted as the formation of a nonnative intermediate state. Analysis by HPLC and SDS-PAGE also indicated the ...
Functions as chaperone and catalyzes the formation of disulfide bonds in substrate proteins, such as COX17 or MICU1 (PubMed:16185709, PubMed:26387864, PubMed:19182799, PubMed:21059946, PubMed:23186364). Required for the import and folding of small cysteine-containing proteins (small Tim) in the mitochondrial intermembrane space (IMS) (PubMed:16185709, PubMed:19182799, PubMed:21059946). Precursor proteins to be imported into the IMS are translocated in their reduced form into the mitochondria (PubMed:16185709, PubMed:19182799, PubMed:21059946). The oxidized form of CHCHD4/MIA40 forms a transient intermolecular disulfide bridge with the reduced precursor protein, resulting in oxidation of the precursor protein that now contains an intramolecular disulfide bond and is able to undergo folding in the IMS (PubMed:16185709, PubMed:19182799, PubMed:21059946). Reduced CHCHD4/MIA40 is then reoxidized by GFER/ERV1 via a disulfide relay system (PubMed:23186364). Mediates formation of disulfide bond in MICU1 ...
Injectable self-healing hydrogels have found broad applications in drug delivery, tissue engineering and controlled 3D cell culture. Recently, cyclic disulfides were found to be useful in cross-linking and stabilizing liposomes by disulfide exchange polymerization, benefiting from the enhanced reactivity of
5.A.1 The Disulfide Bond Oxidoreductase D (DsbD) Family The best characterized member of the DsbD family is DsbD of E. coli (Katzen and Beckwith, 2000; Krupp et al., 2001). The DsbD protein is membrane-embedded with a putative N-terminal TMS plus 8 additional TMSs. The smallest homologues (190 aas with 6 putative TMSs) are found in archaea while the largest are found in both Gram-negative bacteria (758 aas with 9 putative TMSs) and Gram-positive bacteria (695 aas with 6 putative TMSs). In the E. coli DsbD system, electrons are transferred from NADPH in the cytoplasm to periplasmic dithiol/disulfide-containing proteins via an electron transfer chain that sequentially involves NADPH, thioredoxin reductase (TrxB), present in the cytoplasm, thioredoxin (TrxA), also in the cytoplasm, DsbD, the integral membrane constituent of the system, and the periplasmic electron acceptors, DsbC, DsbE (CcmG) and DsbG. All of these last three proteins can donate electrons to oxidized disulfide-containing proteins ...
The inability to form disulfide bonds in the periplasm affects the assembly of complex machinery in the cell envelope. Indeed, loss of DsbA, the primary disulfide bond oxidase in the periplasm, has been shown to block type III secretion in serovar Typhimurium, S. flexneri, P. aeruginosa, and Y. pestis and motility in E. coli and serovar Typhimurium (10, 18, 28, 34, 48, 64) (Fig. 5). But does loss of function indicate a simple defect in assembly? Here we have shown that, in addition to a structural or functional defect conferred by mutations in dsbA, there is a distinct regulatory response. The SPI1 T3SS regulatory circuit responds to the state of disulfide bonds in the periplasm and adjusts expression of the machine components. Our results suggest that loss of DsbA affects SPI1 through four distinct yet overlapping pathways (Fig. 1). First, DsbA inhibits activation of the RcsCDB system (45). Activation of RcsCDB in a dsbA mutant inhibits hilA expression (50) through HilD. Activated RcsCDB also ...
structure and there are five types. It is these heavy chains which enable antibodies to be separated into the five classes (or isotypes) of immunoglobins; IgG, IgA, IgD, IgM and IgE. The way in which the two heavy chains are connected to one another is through disulfide bonds, they are then connected to a light chain by disulfide bonds as well. This therefore creates two identical antigen-binding sites[4]. The regions of the heavy chain includes three constant domains, which are the same for all antibodies, and the one variable domain. The light chains are also composed of a constant domain and a variable domain. The variable regions of the antibodies are where the antigen binding site is located and the constant domain is responsible for the outcome of the antigen[5]. The Fc region is the part of the antibody that binds to cell surface receptors on cells such as macrophages. Finally, the Fab region is primarily known as the location for the antigen binding site[6]. The domains of antibodies are ...
structure and there are five types. It is these heavy chains which enable antibodies to be separated into the five classes (or isotypes) of immunoglobins; IgG, IgA, IgD, IgM and IgE. The way in which the two heavy chains are connected to one another is through disulfide bonds, they are then connected to a light chain by disulfide bonds as well. This therefore creates two identical antigen-binding sites[4]. The regions of the heavy chain includes three constant domains, which are the same for all antibodies, and the one variable domain. The light chains are also composed of a constant domain and a variable domain. The variable regions of the antibodies are where the antigen binding site is located and the constant domain is responsible for the outcome of the antigen[5]. The Fc region is the part of the antibody that binds to cell surface receptors on cells such as macrophages. Finally, the Fab region is primarily known as the location for the antigen binding site[6]. The domains of antibodies are ...
Human interleukin-12p70 (IL-13) is a 15.8 kDa, glycosylated monomeric cytokine with two internal disulfide bonds. It is secreted by a variety of immune cells. IL-13 is involved in a number of biological processes, such as positive regulation of B-cell proliferation, macrophage activation, immunoglobulin production, protein secretion, and phosphorylation of Stat6 protein. IL-13 initially interacts with IL-13 Rα1 to form a low-affinity complex. The formation of this complex triggers association with IL-4 Rα to form a high-affinity complex that also functions as the type 2 IL-4 receptor complex. IL-13 also binds with high affinity to IL-13 Rα2, which is expressed as a soluble intracellular protein, and also on the cell surface. It is involved in a number of disorders including allergic rhinitis, inflammatory bowel disease, and colorectal cancer. The Human IL-13 Kit provides the assay-specific components for the quantitative determination of endogenous IL-13 in human urine, serum, plasma, and ...
We have devised a generally applicable strategy for analysis of protein structure and have applied it to examine the structure of the transmembrane portion of the Tar receptor of Escherichia coli. The basis of our approach is the use of disulfide cross-linking to identify residues that are within close proximity. To generate and test large numbers of cysteine pairs, we used an unusual method of mutagenesis by which cysteine substitutions can be created randomly at a number of targeted codons. Cysteine-substituted proteins encoded by mutagenized genes may be screened directly for disulfide formation within oligomers or, alternatively, different pools of genes may be randomly recombined to generate gene populations with substitutions in multiple regions. Thus, it is possible to detect a variety of disulfide cross-links between and within individual protein molecules. Interactions between the four membrane-spanning stretches of the Tar dimer were probed by measuring the tendency of 48 cysteine ...
MSD offers a range of individual assays utilizing U-PLEX Antibody Sets that provide a rapid and convenient method for measuring biomarkers in complex matrices. The individual assays are offered on MSD GOLD Small Spot Streptavidin Plates and use the same antibody sets and diluents as the U-PLEX multiplex assays. This allows for efficient transfer between the individual assay and a higher throughput multiplex configuration. Typical of assays developed on the MSD platform, the individual assays have high sensitivity, excellent precision, provide up to five-logs of linear dynamic range, and require minimal sample volume. Interleukin-13 (IL-13) is a glycosylated immunoregulatory cytokine with two internal disulfide bonds. IL-13 is secreted by a variety of immune cells. IL-13 is involved in a number of biological processes, such as positive regulation of B-cell proliferation, macrophage activation, immunoglobulin production, protein secretion, and phosphorylation of Stat6 protein. IL-13 initially ...
Many proteins that are exported from the cytosol pass through a membrane channel into the ER in eukaryotes or the extracellular space in prokaryotes (for reviews see Rapoport et al., 1996; Pohlschroder et al., 1997; Matlack et al., 1998; Johnson and van Waes, 1999). The channel is formed by a heterotrimeric complex of proteins called the Sec61 complex in eukaryotes and the SecY complex in bacteria and archaea. The channel has a hydrophilic interior, as shown by electrophysiology and fluorescence lifetime measurements (Simon and Blobel, 1991; Crowley et al., 1994). Previous models assumed that the channel is formed at the interface between three or four copies of the Sec61/SecY complex (Hanein et al., 1996; Beckmann et al., 1997; Hamman et al., 1997; Manting et al., 2000; Menetret et al., 2000). However, the recently solved X-ray structure of the SecY complex from M. jannaschii is of a monomer with no exterior hydrophilic surfaces in the membrane (van den Berg et al., 2004); thus, the channel ...
1MXP: A New Level of Conotoxin Diversity, a Non-native Disulfide Bond Connectivity in alpha -Conotoxin AuIB Reduces Structural Definition but Increases Biological Activity.
Horseradish peroxidase is used in biochemistry applications such as western blots, ELISA and Immunohistochemistry. It is used to amplify a weak signal and increase detectability of a target molecule, such as a protein. HRP labeled immunoglobulins are used as probes for the demonstration of tissue antigens and in enzyme immunoassay (EIA) systems for determination of soluble and insoluble antigens. HRP is the most desired label for antibodies since it is the smallest and most stable of the three most popular enzyme labels (HRP, alkaline phosphatase, and B-galactosidase) and its glycosylation leads to lower non-specific binding. It is also useful for tracing neural connections. These include motor and sensory innervation of peripheral organs, and connections of peripheral nerves, ganglia and individual dorsal roots. HRP can be conjugated to antibodies by several different methods including glutaraldehyde, periodate oxidation, through disulfide bonds, and also via amino and thiol directed ...
A major finding of our present study is that integrin α4β7 can be activated by selectively breaking two conserved disulfide bonds, α4C589-C594 and β7C494-C526, located at the knees of integrin. Interestingly, integrin activated by this mechanism has a unique active conformation that is different from the global conformation induced by Mn2+ stimulation. In addition, activated α4β7 integrin can spontaneously cluster on the cell membrane and trigger integrin outside-in signaling independent of ligand binding.. All integrins contain a large number of disulfide bonds that are generally believed to facilitate protein folding and stabilize three-dimensional structures (Calvete et al., 1991). The two disulfide bonds at the knees of integrin α4β7 are exposed to solution, making them easily accessible to reducing agents. In this study, these two disulfide bonds were selectively reduced by 0.1 mM DTT, which induced the activation of integrin α4β7 and triggered outside-in signaling. Accumulating ...
Sigma-Aldrich offers abstracts and full-text articles by [Martha N Calderon, Carlos A Guerrero, Orlando Acosta, Susana Lopez, Carlos F Arias].
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Immunoglobulin heavy-chain binding protein (BiP, GRP-78) associates tightly in the endoplasmic reticulum (ER) with newly synthesized proteins that are incompletely assembled, have mutant structures, or are incorrectly glycosylated. The function of BiP has been suggested to be to prevent secretion of incorrectly folded or incompletely assembled protein, to promote folding or assembly of proteins, or to solubilize protein aggregates within the ER lumen. Here we examine the interaction of BiP with newly synthesized polypeptides in an in vitro protein translation-translocation system. We find that BiP forms tight complexes with nonglycosylated yeast invertase and incorrectly disulphide-bonded prolactin, but does not associate detectably with either glycosylated invertase or correctly disulphide-bonded prolactin. Moreover, BiP associates detectably only with completed chains of prolactin, not with chains undergoing synthesis. We conclude that BiP recognizes and binds with high affinity in vitro to ...
Bacterial growth and pathogenicity depend on the correct formation of disulfide bonds, a process controlled by the Dsb system in the periplasm of Gram-negative bacteria. Proteins with a thioredoxin fold play a central role in this process. A general feature of thiol-disulfide exchange reactions is the need to avoid a long lived product complex between protein partners. We use a multidisciplinary approach, involving NMR, x-ray crystallography, surface plasmon resonance, mutagenesis, and in vivo experiments, to investigate the interaction between the two soluble domains of the transmembrane reductant conductor DsbD. Our results show oxidation state-dependent affinities between these two domains. These observations have implications for the interactions of the ubiquitous thioredoxin-like proteins with their substrates, provide insight into the key role played by a unique redox partner with an immunoglobulin fold, and are of general importance for oxidative protein-folding pathways in all organisms.
Laminins [(PUBMED:2404817)] are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation. They are composed of distinct but related alpha, beta and gamma chains. The three chains form a cross-shaped molecule that consist of a long arm and three short globular arms. The long arm consist of a coiled coil structure contributed by all three chains and cross-linked by interchain disulphide bonds. Beside different types of globular domains each subunit contains, in its first half, consecutive repeats of about 60 amino acids in length that include eight conserved cysteines [(PUBMED:2666164)]. The tertiary structure [(PUBMED:8648630), (PUBMED:8648631)] of this domain is remotely similar in its N-terminal to that of the EGF-like module. It is known as a LE or laminin-type EGF-like domain. The number of copies of the LE domain in the different forms of laminins is highly variable; from 3 up to 22 copies have been found. A schematic ...
Laminins [(PUBMED:2404817)] are the major noncollagenous components of basement membranes that mediate cell adhesion, growth migration, and differentiation. They are composed of distinct but related alpha, beta and gamma chains. The three chains form a cross-shaped molecule that consist of a long arm and three short globular arms. The long arm consist of a coiled coil structure contributed by all three chains and cross-linked by interchain disulphide bonds. Beside different types of globular domains each subunit contains, in its first half, consecutive repeats of about 60 amino acids in length that include eight conserved cysteines [(PUBMED:2666164)]. The tertiary structure [(PUBMED:8648630), (PUBMED:8648631)] of this domain is remotely similar in its N-terminal to that of the EGF-like module. It is known as a LE or laminin-type EGF-like domain. The number of copies of the LE domain in the different forms of laminins is highly variable; from 3 up to 22 copies have been found. A schematic ...
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Citation: Meng, Y., Moscou, M., Wise, R.P. 2008. Blufensin1 Negatively Impacts Basal Defense in Response to Barley Powdery Mildew. Plant Physiology. 149(1):271-285. Interpretive Summary: Plant diseases are among the greatest deterrents to crop production worldwide. Pathogenic fungi, viruses, bacteria, insects, and nematodes impact agronomic and horticultural crops, as well as commercial and recreational forests. ARS researchers have isolated a novel regulator of disease defense. The new monocot-specific gene encodes a family of small cysteine-rich peptides, designated blufensins. BLUFENSIN1 (BLN1) is highly induced during infection by pathogenic fungi and contains both structural and sequence similarities to knottins, a diverse family of small disulfide-rich proteins characterized by a unique disulfide through disulfide knot. This discovery, also supported by the National Science Foundation-Plant Genome Research Program, establishes a previously unrecognized role for small peptides as negative ...
Sephiroth 20140618 :: DESCRIPTION Sephiroth is a disulfide connectivity pattern predictor based on evolutionary information retrieved from Multiple Sequence Alignments (MSAs). ::DEVELOPER (IB)² - Interuniver
Disulfide bridges are an important structural element in many proteins and peptides. This brochure is a guideline how to plan and execute the synthesis of peptides with one or several disulfide bridges.
1MDK: Solution structure of human thioredoxin in a mixed disulfide intermediate complex with its target peptide from the transcription factor NF kappa B.
colored in yellow) [6] [7] [8] [9]. One structural feature of Pin-II IRD is a disordered loop with triple stranded β sheet scaffold. The disordered solvent exposed reactive loop is anchored by the four conserved disulfide bonds (C4-C41, C7-C25, C8-C37 and C14-C50) [10] [11]. Among the four disulfide bonds, C8-C37 has been found to be very crucial for maintaining active conformation, whereas C4-C41 has an important role in maintaining the flexibility of the reactive loop [12]. Thus, any selective loss of disulfide bond is expected to have evolutionary significance leading to functional differentiation of inhibitors [13]. [A] Functionality: To assess the effect of aa variations on activity and structural stability different biochemical studies and 20 ns MD simulations was performed on IRD structures. Inhibition kinetic studies displayed a sigmoidal pattern with increasing concentrations of the inhibitors suggesting reversible and competitive inhibition with tight binding. IRD-9 turned out to be a ...
An iterator over the disulfide bonds a residue forms. When scoring a pose, a long range energy container must be able to iterate over all the residues which interact with a particular residue. For disulfide bonds, this is either zero or one items depending on whether the residue specified forms a disulfide bond or not.. ...
The meeting was introduced by P. Pontarotti (Marseille, France), who discussed the evolutionary genetics of the MHC based on the ideas of gene co‐option and exon shuffling as the drivers of new functions for existing structures. These ideas about the evolution of the MHC suggest that conserved regions brought into new structures could retain their old (binding) functions. N. Bulleid (Manchester, UK) introduced the topic of MHC class I biosynthesis, describing a semi‐permeable cell system with an intact endoplasmic reticulum that allowed him to address the timing and partners involved in the formation of disulphide bonds between MHC class I and endoplasmic reticulum molecules. He also emphasized the role of the endoplasmic reticulum redox environment and the importance of a transmembrane cysteine residue in associating nascent class I molecules with their appropriate partners. This talk connected to later talks that highlighted misfolding and aberrant disulphide‐bond formation in disease. ...
I didnt even use oxidative environment to trigger disulfide bond formation. Only 1xPBS incubation for 30 min at room temperature, then I saw the dimer on western blot.....Of course this dimer also appears in oxidative enviroment group, but since I can get it using PBS, why bother using oxidative agents?....Afterwards I found out that this dimer doesnt break at RT with DTT or ME, and does break when boiling without DTT ...
Principal Investigator:SHIRATANI Masaharu, Project Period (FY):2009-07-23 - 2014-03-31, Research Category:Grant-in-Aid for Scientific Research on Innovative Areas (Research in a proposed research area), Project Area:Creation of Science of Plasma Nano-Interface Interactions
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(H-Cys-ala-oh)2,(disulfide bond)/ACM20898219 can be provided in Alfa Chemistry. We are dedicated to provide our customers the best products and services.
H-Ala-cys-ser-ser-ser-pro-ser-lys-his-cys-gly-oh,(disulfide bond)/ACM888486235 can be provided in Alfa Chemistry. We are dedicated to provide our customers the best products and services.
✅ Question: Which statement is true? A. a molecule having a covalent bond can be ionic B. a molecule having a covalent bond is always polar C. a molecule having a covalent bond may be polar or nonpolar D. a molecule having a covalent bond i =s always nonpolar
This work has been made available to the staff and students of the University of Sydney for the purposes of research and study only. It constitutes material that is held by the University for the purposes of reporting for HERDC and the ERA. This work may not be downloaded, copied and distributed to any third party ...
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A tripeptide with many roles in cells. It conjugates to drugs to make them more soluble for excretion, is a cofactor for some enzymes, is involved in protein disulfide bond rearrangement and reduces peroxides ...
The very excellent Dr Clive Metcalfe (an ex-post-doc with me) of NIBSC has a PhD project with Prof Paul Dalby at UCL looking at disulphide bond reduction in monoclonal antibodies ...
Enzymes execute a wide variety of functions. For example, they regulate signal transduction via kinases and phosphatases. ATPases generate muscle contraction and active transport. Several enzymes can work together in a specific metabolic pathway (e.g., glycolysis). The common characteristic of enzymes is that they catalyze the chemical modification of specific substrates. Depending on their cellular sub-localization, enzymes can have various preferences toward the presence of reducing agents in biochemical assays. Redox regulation is, like phosphorylation, a covalent regulatory system that controls normal cell function. For example, mitochondria contain the most reducing compartment and are highly sensitive to oxidation. The secretory pathway contains oxidative systems which introduce disulfides into proteins for transport. As opposed to secretory mechanisms, uptake and activation through the endocytic pathway involve reduction of disulfides.. If it is necessary to keep the enzyme of interest ...
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Encourage interaction within the local institute to start building relationships between students in different years of the program. Stronger bonds form when students see each other on a daily basis around campus and once they are established, these bonds can carry over between institutes ...
Double Bond Formation video This Scientific content most probably shows video related to topic: Double Bond Formation. However in few cases, video content could be different than the title.
J. DAVID SCHOFIELD, JOUNI J. UITTO, DARWIN J. PROCKOP; Interchain Disulphide Bonding in Procollagen from Embryonic Chick Tendon Cells and the Formation of the Triple-Helical Structure. Biochem Soc Trans 1 February 1974; 2 (1): 90-93. doi: https://doi.org/10.1042/bst0020090. Download citation file:. ...
TY - JOUR. T1 - Reactive disulfides trigger Ca2+ release from sarcoplasmic reticulum via an oxidation reaction. AU - Zaidi, N. F.. AU - Lagenaur, C. F.. AU - Abramson, J. J.. AU - Pessah, Isaac N. AU - Salama, G.. PY - 1989. Y1 - 1989. N2 - Reactive disulfide compounds (RDSs) with a pyridyl ring adjacent to the S-S bond such as 2,2-dithiodipyridine (2,2-DTDP), 4,4-dithiodipyridine, and N-succinimidyl 3(2-pyridyldithio)propionate (SPDP) trigger Ca2+ release from sarcoplasmic reticulum (SR) vesicles. They are known to specifically oxidize free SH sites via a thiol-disulfide exchange reaction with the stoichiometric production of thiopyridone. Thus, the formation of a mixed S-S bond between an accessible SH site on an SR protein and a RDS causes large increases in SR Ca2+ permeability. Reducing agents, glutathione (GSH) of dithiothreitol reverse the effect of RDSs and permit rapid re-uptake of Ca2+ by the Ca2+, Mg2+-ATPase. The RDSs, 2,2-DTDP, 4,4-dithiodipyridine and SPDP displaced ...
Human serum albumin (HSA) nanoparticles stabilized with intermolecular disulfide bonds Wentan Wang, Yanbin Huang*, Shufang Zhao, Ting Shao and Yi Cheng* Department of Chemical Engineering, Tsinghua University,
Bridging Small Molecules to Modified Bacterial Microparticles Using a Disulphide Linkage: MIS416 as a Cargo Delivery System. . Biblioteca virtual para leer y descargar libros, documentos, trabajos y tesis universitarias en PDF. Material universiario, documentación y tareas realizadas por universitarios en nuestra biblioteca. Para descargar gratis y para leer online.
About the Poster: Optimization of biophysical properties is a critical success factor for the developability of monoclonal antibodies with potential therapeutic applications. The inter-domain disulfide bond between light chain (Lc) and heavy chain (Hc) in human IgG1 lends structural support for antibody scaffold stability, optimal antigen binding, and normal Fc function. Recently, human IgG1l has been suggested to exhibit significantly greater susceptibility to reduction of the inter Lc-Hc disulfide bond relative to the same disulfide bond in human IgG1k. To understand the molecular basis for this observed difference in stability, the sequence and structure of human IgG1l and human IgG1k were compared. Based on this Lc comparison, three single mutations were made in the λ Lc proximal to the cysteine residue, which forms a disulfide bond with the Hc. We determined that deletion of S214 (dS) improved resistance of the association between Lc and Hc to thermal stress. In addition, deletion of this ...
An acidic glycoprotein of MW 23 kDa with internal disulfide bonds. The protein is produced in response to a number of inflammatory mediators by mesenchymal cells present in the hemopoietic environment and at peripheral sites of inflammation. GM-CSF is able to stimulate the production of neutrophilic granulocytes, macrophages, and mixed granulocyte-macrophage colonies from bone marrow cells and can stimulate the formation of eosinophil colonies from fetal liver progenitor cells. GM-CSF can also stimulate some functional activities in mature granulocytes and macrophages ...
TY - JOUR. T1 - Rhodium-catalyzed phosphorylation reaction of water-soluble disulfides using hypodiphosphoric acid tetraalkyl esters in water. AU - Arisawa, Mieko. AU - Fukumoto, Kohei. AU - Yamaguchi, Masahiko. N1 - Funding Information: This research was supported by the Platform Project for Supporting Drug Discovery and Life Science Research from AMED under Grant number JP18am0101100, JSPS KAKENHI Grant number 17K19112, and Tohoku University Center for Gender Equality Promotion (TUMUG).. PY - 2020/4/6. Y1 - 2020/4/6. N2 - RhCl3 catalyzed the exchange reaction of disulfides and hypodiphosphoric acid tetraalkyl esters in water under homogeneous conditions, which indicated the hypodiphosphoric acid tetraalkyl esters to be novel and efficient phosphorylation reagents in water. The reaction was used in the phosphorylation of unprotected glutathione disulfide.. AB - RhCl3 catalyzed the exchange reaction of disulfides and hypodiphosphoric acid tetraalkyl esters in water under homogeneous conditions, ...
The synthesis of architectural polymers with multiple reactive functionalities offers significant promise as platform technologies for development of nano-medicines that require hybrid biomolecule-nanomaterial components. However, there can often be a mismatch in compatibility between the conditions required for the coupling chemistry, while maintaining stability of the biomolecule. This leads to decreased yields and poor functional fidelity. In this report, we describe the synthesis of hyperbranched polymers, where reversible addition fragmentation chaintransfer (RAFT) polymerization is used to control chain molecular weight, end group functionality and the final size of the hyperbranched polymer. Through optimization of the reaction conditions, we demonstrate that branched polymers with controlled size can be synthesized. The subsequent modification of the end-groups within the branched polymer through coupling to small oligonucleotides is then systematically investigated as a function of ...
Since 2010. S. Amram, A. Ganoth, O. Tichon, D. Peer, E. Nachliel, M. Gutman and Y. Tsfadia*, (2014) Structural Characterization of the Drug Translocation Path of MRP1/ABCC1. Isr. J. Chem. 54, 1382-1393, doi: 10.1002/ijch.20130032. A. Ganoth, Y. Tsfadia and R. Wiener, (2013) Ubiquitin: Molecular modeling and simulations. J. Mol. Graph. Model. 46C, 29-40, doi: 10.1016/j.jmgm.2013.09.006. I. Azoulay, N. Kucherenko, E. Nachliel, M. Gutman, A. Azem and Y. Tsfadia*. (2013) Tracking the interplay between bound peptide and the lid domain of DnaK, using Molecular Dynamics. Int. J. Mol. Sci. 14, 12675-12695, doi: 10.3390/ijms140612675 L. Levin, E. Zelzion, E. Nachliel--, M. Gutman, Y. Tsfadia*- and Yulia Einav*, (2013) A Single Disulfide Bond Disruption in the β3 Integrin Subunit Promotes Thiol/Disulfide Exchange, a Molecular Dynamics Study. Plos One. 8, Issue 3, e59175. Azem A*, Tsfadia Y*, Hajouj O, Shaked I and Daniel E. (2010) Cross-linking with bifunctional reagents and its application to the study ...
TY - JOUR. T1 - Denatured and reversibly cationized p53 readily enters cells and simultaneously folds to the functional protein in the cells. AU - Murata, Hitoshi. AU - Sakaguchi, Masakiyo. AU - Futami, Junichiro. AU - Kitazoe, Midori. AU - Maeda, Takashi. AU - Doura, Hideki. AU - Kosaka, Megumi. AU - Tada, Hiroko. AU - Seno, Masaharu. AU - Huh, Nam Ho. AU - Yamada, Hidenori. PY - 2006/5/16. Y1 - 2006/5/16. N2 - Cationization is a powerful strategy for internalizing a protein into living cells. On the other hand, a reversibly cationized denatured protein through disulfide bonds is not only soluble in water but also able to fold to the native conformation in vitro. When these advantages in cationization were combined, we developed a novel method to deliver a denatured protein into cells and simultaneously let it fold to express its function within cells. This in-cell folding method enhances the utility of recombinant proteins expressed in Escherichia coli as inclusion bodies; that is, the ...
Protein which possesses at least one active center which mediates its participation in redox reactions, usually via reversible oxidation of a cysteine residue leading to a cysteine-sulfenic acid that can either be stabilized, or react with an unmodified cysteine residue and form a stable but reversible disulfide bond ...
ChemInform Abstract: Incorporating Disulfide Cross-Links at the Terminus of Oligonucleotides via Solid-Phase Nucleic Acid Synthesis.|span||/span| | S. E. OSBORNE; A. D. ELLINGTON | download | BookSC. Download books for free. Find books
Transmembrane α-helical proteins are unusually stable judging from thermal denaturation studies, because they do not unfold completely within the membranes (the complete unfolding would require breaking down too many α-helical H-bonds in the nonpolar media). On the other hand, these proteins easily misfold, due to non-native aggregation in membranes, transition to the molten globule states, formation of non-native disulfide bonds, or unfolding of peripheral regions and nonregular loops that are locally less stable. It is also important to properly define the unfolded state. The unfolded state of membrane proteins in detergent micelles is different from that in the thermal denaturation experiments. This state represents a combination of folded hydrophobic α-helices and partially unfolded segments covered by the detergent. For example, the unfolded bacteriorhodopsin in SDS micelles has four transmembrane α-helices folded, while the rest of the protein is situated at the micelle-water ...
The type IV pili (T4P) is a major virulence factor of Pseudomonas aeruginosa (P. aeruginosa) that is associated with primary adhesion, biofilm formation and twitching motility. This study focuses on the introduction of a novel biologically active subunit vaccine derived from the disulfide loop (DSL) of P. aeruginosa pilin. We investigated the ...
Disulfide bond (DSB) analysis and hydrogen deuterium exchange (HDX) have emerged as technologies that can be employed to gain insights into protein structure. These insights are critical for determining structural similarity for biosimilars, or for monitoring protein stability during drug development. The tertiary structure of therapeutic proteins is key to their activity and stability. Research and development labs require technology capable of automated DSB analysis in biopharmaceuticals, based on a single digest of the unreduced protein and without prior knowledge of enzyme specificity or native DSBs. Due to the complexity of these proteins and the fact that they will contain multiple disulfide bonds, analysis is a challenge, often requiring several LC-MS runs with the tryptic digests from reduced and non-reduced protein and a manual comparison of these two analyses. ...
This thesis describes three separate but related projects exploring how herpes simplex virus 1 (HSV-1) induces and copes with a pro-oxidant environment during infection. We found that the UL6 portal ring, the conduit responsible for the uptake and release of viral DNA, required disulfide bonds for ring formation and stability. Mutagenesis studies revealed that these disulfide bonds might be mediated by cysteines 166 and 254. We next examined the protein UL32 as a potential virally encoded oxidoreductase. UL32 contains three C-X-X-C motifs reminiscent of proteins that regulate disulfide bond formation. Mutation of two of these C-X-X-C motifs abrogated protein function. We used a thiol-alkylation assay to show that viral capsid proteins, including UL6, had altered disulfide bond profiles in the absence of UL32, suggesting that UL32 influences disulfide bond formation in capsid proteins during assembly and maturation. We then confirmed that HSV induces oxidation using a redox-sensitive GFP probe. We also
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As noted, cysteine is characterized by the presence of a thiol (sulphydry) group (-SH). Since thiol groups can undergo reduction (redox) reactions, cysteine can undergo redox reactions. Oxidation of cysteine can produce a disulfide bond with another thiol. A disulfide bond, also called a SS-bond or disulfide bridge, is a single covalent bond derived from the coupling of thiol groups. The overall connectivity is C-S-S-C.. That is, when cysteine is oxidized it can form cystine, which is two cysteine residues joined by a disulfide bond (cys-S-S-cys) between the -SH group. This reaction is reversible, as reduction of this disulphide bond regenerates two cysteine molecules. (Further oxidation can produce sulphfinic or sulfonic acids.). The disulphide bonds of cystine are crucial to defining the structures of many proteins. Disulfide bonds play an important role in the folding and stability of some proteins, by stabilizing the folded form. Extracellularly, by crosslinking proteins, cysteines increase ...
In this study, we aimed to examine dynamic thiol/disulfide homeostasis in type 1 diabetes mellitus (T1DM) and identify the factors associated with thiol oxidation. Thirty-eight subjects (18 male, 20 female) diagnosed with T1DM and 38 (17 male, 21 female) healthy volunteers without any known diseases were included in the study. Thiol/disulfide homeostasis concentrations were measured by a newly developed method (Erel & Neselioglu) in this study. After native thiol, total thiol and disulfide levels were determined; measures such as disulfide/native thiol, disulfide/total thiol, and native thiol/total thiol were calculated. In T1DM patients, compared to the control group, disulfide (p = 0.024), disulfide/native thiol (p < 0.001), and disulfide/total thiol (p < 0.001) were determined higher, while native thiol (p = 0.004) and total thiol (p < 0.001) levels were much lower. In the patient group, a positive correlation was determined between c-reactive protein (r = 325, p = 0.007; r = 316, p = 0.010, ...
The ORP100S therapeutic strategy is based on supplementing the activity of the human protein thioredoxin-1 (TXN1), which is normally secreted onto the airway surface where it acts selectively to modify certain types of protein disulfide bonds formed between cysteine amino acids. The thioredoxin mechanism targets airway mucus to keep it at a normal viscosity (thickness and stickiness) and able to maintain the essential process of mucus clearance that sweeps the lungs clean of inhaled material and excess fluid. Thioredoxin also targets regulatory (allosteric) disulfide bonds on immune system proteins as part of a natural homeostatic mechanism to prevent excessive release of cytokines in response to inflammatory stimulus. Together, impaired airway clearance and abnormally elevated cytokine release comprise key pulmonary manifestations of moderate to severe COVID-19 that can lead to systemic disease and poor outcomes ...
Disulfide rich peptides have gained significant attention recently due to their incredible biological stability and tolerance to epitope grafting. This class of peptides is often folded in solution, assuming the desired disulfide bond pattern correlates with the most thermodynamically stable structure. Sometimes though, especially for chemically synthesized cysteine rich peptides, this is not the case. The result is a complex mixture of peptides with varying disulfide bonding patterns and identical mass ...
The LIP-6 MAb was produced against the undifferentiated cell line bh2-1 and recognizes an antigen expressed on all pre-B and B cell lines tested and some myeloid lineage lines. FACS analysis of normal tissues showed that LIP-6 is expressed on B lineage cells at all stages of differentiation, from bone marrow pre-B to plasma cells. T cells and thymocytes are LIP-6-, and splenic CD11b+ cells are heterogeneous for LIP-6 expression. The LIP-6 MAb was shown to precipitate a major 75-kDa and a minor 85-kDa protein under reducing conditions and a large protein of | 240 kDa under nonreducing conditions. Removal of N-linked sugars from the reduced lysates resulted in a single 65-kDa protein, suggesting that there is differential glycosylation of a single 65-kDa protein that forms disulfide-linked multimers. Finally, the LIP-6 antigen was shown not to be linked to the cell surface via a GPI linkage.
Transforming growth factor beta 1 (TGF-β1) is a member of the transforming growth factor beta superfamily of cytokines. TGF-β1 precursor contains a pro-region (latency associated peptide or LAP), and C-terminal region that becomes active TGF-β1 upon activation. Both LAP and TGF- β1 exist as homodimers in circulation, but the disulfide-linked homodimers of LAP and TGF-β1 remain non-covalently associated, forming the small latent TGFβ1 complex. The large latent TGF- β1 Complex contains a third component, the latent TGF-β binding protein (LTBP), which is linked to LAP by a single disulfide bond. LTBP does not confer latency, but is required for efficient secretion of the complex to extracellular sites. Free active TGF-β1 can be released by many factors, including enzymes and low or high pH. It has diverse biological functions in multiple cellular processes, with its intracellular signaling pathways being associated with regulation of proliferation and differentiation to various cell ...
Which is the correct bond structure? Im looking specifically at the condensation polymerization of diamine and diacarboxylic acid to form nylon.. And also, I see online that lots of bond structures (like NH2 and COOH) are prefixed with a dash, so theyd appear like -NH2 and -COOH. Is this just a personal preference, or is there a more elaborate reason behind this?. Im currently doing the GCSEs.. Thanks. ...
FUNCTION: [Summary is not available for the mouse gene. This summary is for the human ortholog.] This gene encodes a type II transmembrane glycoprotein that is the highly polymorphic Kell blood group antigen. The Kell glycoprotein links via a single disulfide bond to the XK membrane protein that carries the Kx antigen. The encoded protein contains sequence and structural similarity to members of the neprilysin (M13) family of zinc endopeptidases. [provided by RefSeq, Jul 2008 ...
This gene encodes a type II transmembrane glycoprotein that is the highly polymorphic Kell blood group antigen. The Kell glycoprotein links via a single disulfide bond to the XK membrane protein that carries the Kx antigen. The encoded protein contains sequence and structural similarity to members of the neprilysin (M13) family of zinc endopeptidases ...
Several conclusions can be drawn:. (i) The sequence of PHF6 at the beginning of the third repeat (exon 11) is present in all τ isoforms and provides an explanation why all τ isoforms can form PHFs. The counterpart PHF6* lies at the beginning of R2 (exon 10) and is therefore present only in τ isoforms containing four repeats. If the two hotspots for β-sheet formation operated in a cooperative fashion, they could possibly enhance PHF assembly, and this might explain why PHF formation is enhanced in dementias where the four-repeat isoforms are overrepresented (e.g., FTDP-17; see refs. 31-33).. (ii) Dimerization of τ via oxidation of Cys-322 into an intermolecular disulfide bridge strongly promotes PHF assembly (5). The results shown here argue that the peptide containing Cys-322 (peptide 318-335; Fig. 5) does not promote PHF assembly by itself. However, dimerization at Cys-322 could bring two PHF6 motifs into close vicinity, which would facilitate β-sheet interactions. In this view, ...
We will establish the nature of two novel protein disulfide bond-forming pathways found in certain bacteria and archaea. E. coli and many other bacteria use two...
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Protein disulfide isomerase (PDI) is a multifunctional protein that facilitates the formation of correct disulfide crosslinks between cysteine residues during the early stages of protein folding and secretion in the endoplasmic reticulum
Correct localization to lipid rafts is essential for LAT (linker for activation of T cells)-mediated signaling through the T cell antigen receptor (TCR). Under conditions of chronic oxidative stress, T cells are hyporesponsive to stimuli. For example, in rheumatoid arthritis (RA), T cell insensitivity is thought to contribute to the disorder. Grinhuis et al. found that LAT localization in T cells is perturbed during chronic oxidative stress and results in decreased signaling outputs. LAT isolated from T cells treated with an inhibitor of glutathione (GSH) synthesis exhibited faster migration than LAT from untreated T cells under nonreducing conditions in gel electrophoresis. This suggested that LAT might form intramolecular disulfide bonds under conditions of chronic oxidative stress. Mutational analysis of Cys residues on LAT revealed that C117S or C26/29S mutants were partially insensitive to chronic oxidative stress (presumably because they could not become oxidized and form disulfide ...
Thioredoxins (TRXs) are small (approximately 12 kD), ubiquitous oxidoreductases that mediate the dithiol-disulfide exchange of Cys residues, thereby modulating the function and stability of their target proteins (Schürmann and Buchanan, 2008). The short peptide motif WC(G/P)PC, with its two conserved Cys residues, has been characterized as the conserved redox-active site of TRXs (Jacquot et al., 1997; Buchanan and Balmer, 2005; Meyer et al., 2008). In chloroplasts, the disulfide bonds of TRXs can be reduced by ferredoxin-TRX reductase receiving the receipt of electrons from the photoreduced ferredoxin. Subsequently, the reduced TRX acts to reduce the disulfide groups of its target proteins (Dai et al., 2000, 2007; Schürmann and Buchanan, 2008). The five different classes of chloroplast TRXs have been characterized as TRX-F, TRX-M, TRX-X, TRX-Y, and TRX-Z in Arabidopsis (Arabidopsis thaliana). The two classes of TRX-M and TRX-F consist of four and two separate members, respectively, and are ...
There is a trigonal planar arrangement of bonds around the carbon atom of the carbonyl group (,C=O) because there are three groups of electrons involved.. There are two C-R σ bonds between the carbon and the H/alky/aryl group and the σ plus π of the carbon - oxygen bond of the carbonyl C=O group which spread out in an angular manner of 120o to minimise repulsion.. The planarity of this bond arrangement means that there is a 50:50 chance of the nucleophile attacking on either side of carbon - this has consequences if the product is an optical R/S isomer. To envisage this, consider the right-hand side of the diagram and imagine the C=O in the plane of the screen and the black bond ▲ pointing directly towards you and the grey bond▼ pointing directly away from you.. This is further discussed with extra mechanism diagrams in section 6.4.6. ...
Disulfide bonds are important for protein stability, but little is known about how they are formed in Gram-positive bacteria. By investigating disulfide bond formation in Streptococcus gordonii, a potential live vaccine vector, I hope to contribute to our understanding of protein production in this group of organisms, and to the development of novel S. gordonii based vaccines.. ...
DTT or Clelands Reagent reduces disulfides to their corresponding thiols. It is used at low concentrations to stabilize enzymes containing free sulphydryl groups. Higher concentrations of DTT are used to cleave disulphide linkages in polypeptides and to facilitate protein denaturation by detergents or chaotropic agents. ...
Similarly, cysteine directed PIK-75 cross linking was employed in our present study to map the binding interface of Bcl xL subunits in lipids. Especially, Bcl xL was incubated with folds of LUV followed by reaction with membrane permeant oxidative, CuP. As shown in Inhibitors A , two main bands close to kDa and kDa, corresponding to two isoforms of BclxL disulfide bond dimers , seem after incubation in the liposomebound Bcl xL with CuP. This consequence is consistent which has a previous report that Bcl forms SDS resistant dimer soon after incubation with liposomes at pH Because the protein was incubated with folds of LUV in advance of the oxidization, the disulfide bond should be formed within the liposomes. Actually, only negligible disulfide bond dimer was detected from the absence of LUV , confirming that the disulfide bond dimer is formed in liposomes. As Bcl xL has only one cysteine residue and found within the helix , it must be with the binding interface of Bcl xL subunits in membranes. ...
Data on 6,500 pesticides, insecticides and herbicides including toxicity, water pollution, ecological toxicity, uses and regulatory status.
I need to resolve a problem with a denatured a protein with 2-mercaptoethanol and 8 M urea . I need to study quenching on Trp and sadly 2-mercaptoethanol its a quencher. So i need to obtain a denature protein without disulfide bonds in 8 M urea but without 2-mercaptoethanol. I tought of making an ultrafiltration by keeping the volume constant and the solution of 8 M urea. However, my concern is if I change the reducing media the protien will oxidise the Cys again ...
Protocols for postsynthetic modification of 2‐amino‐containing oligoribonucleotides with either an alkyl‐phenyl disulfide or an alkyl thiol group are described
Characterization of post-translational modifications in full-length human BMP-1 confirms the presence of a rare vicinal disulfide linkage in the catalytic domain and highlights novel features of the EGF domain. ...
Disulfide bonds play an important role in protein folding and structure stability. Accurately predicting disulfide bonds from protein sequences is important for modeling the structural and functional characteristics of many proteins.
Figure 1 is a chromatogram of the headspace above the culture after 13 hours of continuous purging. The culture is in the log phase of growth. Figure 2 is a chromatogram of the headspace above the culture after 20 hours of continuous purging. The culture is in the stationary phase of growth. Figure 3 is a chromatogram of the headspace above the culture after 106 hours of continuous purging. The culture is in the late stationary phase of growth. Figure 4 is a plot of the analyses from a single experiment carried out over 100 hours. The relative headspace concentration of dimethyl disulfide (DMDS) and dimethyl diselenide (DMDSe) is shown. This time course experiment last over 100 hours. The results of a single time course experiment for Rhodobacter sphaeroides are shown in Figure 5. The experiment lasted approximately 180 hours. The top graph in this figure shows the cultures optical density (OD) at 660 nm as a measure of biomass and the ratio of optical density at 875 and 660 nm as a measure of ...
Photochemistry and Photobiology publishes on photoscience, like primary interaction of light with molecules, cells, and tissue to biological responses.
Thiol SS Serinol Dipod DTSPA) is a disulfide-containing modifier designed to functionalize synthetic DNA or RNA with multiple thiol groups and can be incorporated at any position of the oligonucleotide. Each DTPA addition leads to two thiol groups. This modifier was designed for optimal tethering of oligonucleotides to a gold surface but it can also be used for multiple reactions with maleimides and other thiol-specific derivatives ...
The ζ subunit is a 16 kDa surface molecule associated with the T cell receptor. Its expression is restricted to T lymphocytes and NK cells. In T lymphocytes, the ζ subunit is expressed as a disulfide-linked homodimer of 32 kDa or as a disulfide-linked heterodimer with a 21 kDa subunit designated η.
The ζ subunit is a 16 kDa surface molecule associated with the T cell receptor. Its expression is restricted to T lymphocytes and NK cells. In T lymphocytes, the ζ subunit is expressed as a disulfide-linked homodimer of 32 kDa or as a disulfide-linked heterodimer with a 21 kDa subunit designated η.
... is the S-oxide of a disulfide, and a thiosulfonate, R−S(O)2−S−R, is the S,S-dioxide of a disulfide. All of these compounds are ... Thiols, disulfides, polysulfides[edit]. Thiol groups contain the functionality R−SH. Thiols are structurally similar to the ... Disulfides R−S−S−R with a covalent sulfur to sulfur bond are important for crosslinking: in biochemistry for the folding and ... but include the important compounds carbon disulfide, carbonyl sulfide, and thiophosgene. Thioketones (RC(=S)R′) are uncommon ...
Carbon disulfide derivatives[edit]. Boiled with carbon disulfide, it gives sulfocarbanilide (diphenylthiourea) (CS(NHC6H5)2), ...
Fullerenes are sparingly soluble in aromatic solvents such as toluene and carbon disulfide, but insoluble in water. Solutions ... When C60 is mixed with a disulfide RSSR, the radical C60SR• forms spontaneously upon irradiation of the mixture. ...
1.4.4: disulfide acceptor. *Glycine cleavage system. 1.4.99: other acceptors. *D-amino acid dehydrogenase ...
Researcher D. G. Walker of the University of Birmingham determined the presence of two specific enzymes in adult guinea pig liver, both of which catalyze the phosphorylation of glucose to glucose 6 phosphate.[dubious - discuss] The two enzymes have been identified as a specific glucokinase (ATP-D-glucose 6-phosphotransferase) and non-specific hexokinase (ATP-D-hexose 6-phosphotransferase). Hepatic cell is freely permeable to glucose, and the initial rate of phosphorylation of glucose is the rate-limiting step in glucose metabolism by the liver (ATP-D-glucose 6-phosphotransferase) and non-specific hexokinase (ATP-D-hexose 6-phosphotransferase).[11] The role of glucose 6-phosphate in glycogen synthase: High blood glucose concentration causes an increase in intracellular levels of glucose 6 phosphate in liver, skeletal muscle and fat (adipose) tissue. (ATP-D-glucose 6-phosphotransferase) and non-specific hexokinase (ATP-D-hexose 6-phosphotransferase). In liver, synthesis of glycogen is directly ...
Hydrogen disulfide. Dioxygen difluoride Except where otherwise noted, data are given for materials in their standard state (at ... Diphosphane and hydrogen disulfide exhibit only weak hydrogen bonding and have little chemical similarity to hydrogen peroxide ...
Carbon disulfide Liquid CS2 89.41 Carbon disulfide Gas CS2 116.7 ...
Ruthenium disulfide Other cations. Osmium(IV) oxide Related ruthenium oxides. Ruthenium tetroxide ...
Disulfide bond reducersEdit. Agents that break disulfide bonds by reduction include:[citation needed] ... Covalent interactions between amino acid side-chains (such as disulfide bridges between cysteine groups) ... an injury-induced aggregation event that disulfide crosslinks proteins and facilitates their removal by plasmin". Cell Reports ...
Carbon disulfide derivativesEdit. Boiled with carbon disulfide, it gives sulfocarbanilide (diphenylthiourea) (CS(NHC6H5)2), ...
Disulfide bond reducersEdit. Agents that break disulfide bonds by reduction include:[citation needed] ... Covalent interactions between amino acid side-chains (such as disulfide bridges between cysteine groups) ... "Nucleocytoplasmic coagulation: an injury-induced aggregation event that disulfide crosslinks proteins and facilitates their ...
"Structure/function analysis of a critical disulfide bond in the active site of L-xylulose reductase". Cell. Mol. Life Sci. 66 ( ...
1.1.4: disulfide as acceptor. *Vitamin K epoxide reductase. *Vitamin-K-epoxide reductase (warfarin-insensitive) ...
1.1.4: disulfide as acceptor. *Vitamin K epoxide reductase. *Vitamin-K-epoxide reductase (warfarin-insensitive) ...
1.1.4: disulfide as acceptor. *Vitamin K epoxide reductase. *Vitamin-K-epoxide reductase (warfarin-insensitive) ...
1.1.4: disulfide as acceptor. *Vitamin K epoxide reductase. *Vitamin-K-epoxide reductase (warfarin-insensitive) ...
1.1.4: disulfide as acceptor. *Vitamin K epoxide reductase. *Vitamin-K-epoxide reductase (warfarin-insensitive) ...
with sulfur to form carbon disulfide and with steam in the coal-gas reaction:. C(s) + H2O(g) → CO(g) + H2(g).. Carbon combines ... Carbon disulfide (CS. 2) is similar.[23]. The other common oxide is carbon monoxide (CO). It is formed by incomplete combustion ...
1.1.4: disulfide as acceptor. *Vitamin K epoxide reductase. *Vitamin-K-epoxide reductase (warfarin-insensitive) ...
Molybdenum disulfide - MoS2. *Molybdenum hexacarbonyl - Mo(CO)6. *Molybdenum hexafluoride - MoF6 ...
lithium-iron disulfide). LiFeS2. Li. FeS2. 1.8. 1.5. 1.07. Expensive.. Used in 'plus' or 'extra' batteries.. 337[68] ... "Lithium Iron Disulfide Handbook and Application Manual" (PDF). energizer.com. Retrieved 20 September 2018.. ...
X. Intrachain disulfide bonds". Biochemistry. 9 (16): 3188-96. doi:10.1021/bi00818a011. PMID 4923144.. ... and the disulfide bridges (author's transl)]". Hoppe-Seyler's Z. Physiol. Chem. 357 (11): 1515-40. PMID 1002129.. ...
proteïne-disulfide reductase (glutathion) Ja 1.8.4.B3 thioredoxin-independent methionine sulfoxide reductases B Ja ...
... contains three disulfide bridges.[5] Mode of action[edit]. Charybdotoxin occludes the pore of calcium-activated ...
Carbon disulfide. 2.6 Mylar. 3.1[2] Paper, printing, 200 kHz,. 1.4[3] ...
Witt D (2008). "Recent developments in disulfide bond formation". Synthesis. 2008 (16): 2491-2509. doi:10.1055/s-2008-1067188. ...
... also has a transferrin iron-bound receptor; it is a disulfide-linked homodimer.[9] In humans, each monomer consists ...
There are also no disulfide bridges. As a result, it has relatively little tertiary structure. It is relatively hydrophobic, ...
Carbon forms disulfides and diselenides. Silicon forms several hydrides; two of them are SiH4 and Si2H6. Silicon forms ... Silicon also forms a dioxide and a disulfide. Silicon nitride has the formula Si3N4. Germanium forms five hydrides. The first ... Germanium bonds to all natural single chalcogens except polonium, and forms dioxides, disulfides, and diselenides. Germanium ...
Sb2O3 Fool's gold - a mineral, iron disulfide or pyrite; can form oil of vitriol on contact with water and air. Fulminating ... or ferrous sulfate) Marcasite - a mineral; iron disulfide. In moist air it turns into green vitriol, FeSO4. Rouge/Crocus/ ... Used for glass coloring Quicksilver - Mercury Realgar - arsenic disulfide, an ore of arsenic Red Vitriol - cobalt sulfate ...
... disulfide species". A disulfide ensemble is a grouping of all disulfide species with the same number of disulfide bonds, and is ... Disulfides where the two R groups are the same are called symmetric, examples being diphenyl disulfide and dimethyl disulfide. ... This process of disulfide rearrangement (known as disulfide shuffling) does not change the number of disulfide bonds within a ... for disulfide species having one, two, etc. disulfide bonds. Thus, the (26-84) disulfide species belongs to the 1S ensemble, ...
... hydrogen disulfide adds to alkenes to give disulfides and thiols. The deuterated form of hydrogen disulfide DSSD, has a similar ... Hydrogen disulfide has been described as "having a severe and irritating odour" that is similar to camphor or SCl 2, causing " ... Hydrogen disulfide is the inorganic compound with the formula H2S2. This hydrogen chalcogenide is a pale yellow volatile liquid ... Hydrogen disulfide can be synthesised by dissolving alkali metal or alkaline earth metal polysulfides in water. When the ...
... disulfide species". A disulfide ensemble is a grouping of all disulfide species with the same number of disulfide bonds, and is ... Organic disulfides[edit]. A selection of disulfides FeS2,. "fools gold". S2Cl2,. a common industrial chemical. cystine,. ... a common organic disulfide. Symmetrical disulfides are compounds of the formula R2S2. Most disulfides encountered in organo ... This process of disulfide rearrangement (known as disulfide shuffling) does not change the number of disulfide bonds within a ...
Selenium disulfide was approved for medical use in the United States at least as early as 1951.[3] It is on the World Health ... Selenium disulfide can cause discoloration of the hair and alter the color of hair dyes. It may also discolor metallic ... Selenium disulfide, also known as selenium sulfide, is a medication used to treat pityriasis versicolor, seborrhoeic dermatitis ... Selenium disulfide is sold as an antifungal agent in shampoos for the treatment of dandruff and seborrheic dermatitis ...
Workers may be harmed by carbon disulfide. The level of exposure depends upon the dose, duration, and work being done. ... Carbon disulfide (CS2) is a colorless liquid with an ether-like odor. Exposure can cause dizziness, poor sleep, headache, ... EPA Acute Exposure Guideline Levels (AEGLs): Carbon Disulfideexternal icon. *EPA Chemistry Dashboard: Carbon Disulfideexternal ... IPCS INCHEM (CICADS) 46: Carbon Disulfideexternal icon. *IPCS INCHEM Environmental Health Criteria 10: Carbon Disulfideexternal ...
Carbon disulfide has been found in at least 210 of the 1,430 National Priorities List sites identified by the Environmental ... Exposure to carbon disulfide can occur by breathing it in the air and by drinking water or eating foods that contain it. ... What is carbon disulfide?. Pure carbon disulfide is a colorless liquid with a pleasant odor that is like the smell of ... How can carbon disulfide affect my health?. At very high levels, carbon disulfide may be life-threatening because of its ...
Evacuate danger area! Consult an expert! Remove all ignition sources. Personal protection: filter respirator for organic gases and vapours adapted to the airborne concentration of the substance. Ventilation. Do NOT wash away into sewer. Do NOT let this chemical enter the environment. Collect leaking and spilled liquid in sealable containers as far as possible. Absorb liquid in sand or inert absorbent. Carefully collect remainder in sealable containers. Store and dispose of according to local regulations ...
... is a one-carbon compound (CHEBI:64708) carbon disulfide (CHEBI:23012) is a organosulfur compound ... CHEBI:23012 - carbon disulfide. Main. ChEBI Ontology. Automatic Xrefs. Reactions. Pathways. Models. ...
Toxicological profile for Carbon Disulfide. Atlanta, GA: U.S. Department of Health and Human Services, Public Health Service. ...
Other names: Propyl disulfide; Dipropyl disulfide; 4,5-Dithiaoctane; Dipropyl disulphide; (n-C3H7S)2; n-Propyl disulfide; di-n- ... Propyl disulfide; 1-(Propyldisulfanyl)propane; NSC 75122 * Permanent link for this species. Use this link for bookmarking this ...
Other names: 2,3-Dithiabutane; Methyl disulfide; (Methyldithio)methane; Dimethyl disulfide; Dimethyl disulphide; (CH3S)2; UN ... Equilibrium studies on the disproportionation reaction between some dialkyl disulfides, Acta Chem. Scand., 1960, 14, 1509-1514 ...
Appendix I - Air Sampling Method for Carbon Disulfide. X. Appendix II - Analytical Method for Carbon Disulfide. 77-156F.PDF (28 ... I. Recommendations for a Carbon Disulfide Standard. 77-156B.PDF (21 pages, 697K)pdf icon. ... Criteria for a Recommended Standard: Occupational Exposure to Carbon Disulfide. ... Appendix III - Method of Biologic Monitoring for Carbon Disulfide: Iodine-Azide Test. ...
The exposure under study was carbon disulfide, a chemical used in rubber chemicals department. ... Carbon disulfide exposures at the plant were not found at levels associated with heart disease and the chemical was removed ... Tire and Rubber Company (1) (Carbon disulfide Exposure). 2001. Study Background. NIOSH conducted a study of workers at a tire ... Some studies suggest that carbon disulfide, a chemical used in making rubber chemicals, may increase the risk of heart disease ...
This chapter provides the diffusion coefficient of hexane in carbon disulfide at different concentrations measured using ... Winkelmann J. (2018) Diffusion coefficient of hexane in carbon disulfide. In: Lechner M.D. (eds) Diffusion in Gases, Liquids ... This chapter provides the diffusion coefficient of hexane in carbon disulfide at different concentrations measured using ...
2013) Tungsten disulfide nanotubes reinforced biodegradable polymers for bone tissue engineering. Acta Biomater 9(9):8365-8373. ... Diameter-dependent wetting of tungsten disulfide nanotubes. Ohad Goldbart, Sidney R. Cohen, Ifat Kaplan-Ashiri, Polina ... Here, we present a comprehensive wetting study of individual tungsten disulfide nanotubes by water. We reveal the nature of ... We have studied the wetting of individual, size-selected tungsten disulfide nanotubes, both experimentally and theoretically. ...
Tetraisobutylthiuram disulfide molecules of one optical configuration form sheets in the plane of the a and b axes. Inversion ... Tetrakis(2-methylpropyl)thioperoxydicarbonic diamide, or tetraisobutylthiuram disulfide, C18H36N2S4, crystallizes in a general ... position in the triclinic space group P-1 but shows pseudo-C2 symmetry about the disulfide bond. The C-S-S-C torsion angle [− ...
Here, we report the synthesis of the metallic 2H phase of niobium disulfide with additional niobium (2H Nb1+xS2, where x is ~ ... The metallic 2H phase of niobium disulfide now exhibits enhanced current densities versus a reversible hydrogen electrode. ... Here, we report the synthesis of the metallic 2H phase of niobium disulfide with additional niobium (2H Nb1+xS2, where x is ~ ... Yang, J., Mohmad, A.R., Wang, Y. et al. Ultrahigh-current-density niobium disulfide catalysts for hydrogen evolution. Nat. ...
... is a multifunctional protein that facilitates the formation of correct disulfide crosslinks between cysteine residues during ... The catalysis of disulfide formation relies almost entirely on the high reactivity of PDIs active site disulfides. However, ... Catalysis of disulfide isomerisation. Disulfide isomerisation is initiated by attack of the nucleophilic cysteine of the PDI. ... Protein disulfide isomerase (PDI) is a multifunctional protein that facilitates the formation of correct disulfide crosslinks ...
Disulfide bonds in wheat proteins are major factors that determine the properties of the proteins and their functionality in ... Disulfide Bond Bread Wheat Wheat Flour Mercuric Chloride Glutenin Subunit These keywords were added by machine and not by the ... Disulfide bonds in wheat proteins are major factors that determine the properties of the proteins and their functionality in ... Huebner F.R., Bietz J.A., Wall J.S. (1977) Disulfide Bonds: Key to Wheat Protein Functionality. In: Friedman M. (eds) Protein ...
Inter-subunit disulfide bonds also produced some ASIC1a complexes larger than trimers. Inter-subunit disulfide bond formation ... ASIC1a Forms Inter-Subunit Disulfide Bonds in Vivo.. To learn if ASIC1a forms inter-subunit disulfide links in vivo, we blotted ... ASIC1a Forms Inter-Subunit Disulfide Bonds.. To learn whether inter-subunit disulfide bonds might contribute to the multimeric ... of surface subunits were linked by inter-subunit disulfide bonds. These data indicate that disulfide linkage between ASIC1a ...
... has discovered an optoelectronic application for molybdenum disulfide (MoS2), a 2-dimensional semiconductor material, according ... has discovered an optoelectronic application for molybdenum disulfide (MoS2), a 2-dimensional semiconductor material, according ...
Disulfide content of reduced hen egg white and human milk lysozymes during the folding process. *Perraudin J ... Following disulfide bond formation, under identical conditions, similar products were found during the folding of both ... Perraudin, J. P., Guillard, R., Prieels, J. P., Torchia, T., & Thierry, D. (1983). Disulfide content of reduced hen egg white ...
Molybdenum disulfide (MoS2) is a hexagonal layer structured material. The MoS2 layers, each of which consists of a layer of ... R. N. Viswanath and S. Ramasamy, "Preparation and isochronal sintering behavior of molybdenum disulfide compound," Journal of ... R. R. Chianelli, E. B. Prestridge, T. A. Pecoraro, and J. P. Deneufville, "Molybdenum disulfide in the poorly crystalline "rag ... K. I. Tanaka and T. Okuhara, "Regulation of intermediates on sulfided nickel and molybdenum disulfide catalysts," Catalysis ...
Role of Disulfide Bridges Formed in the Luminal Domain of ATF6 in Sensing Endoplasmic Reticulum Stress Satomi Nadanaka, Tetsuya ... Intramolecular Disulfide Bonds of the Prolactin Receptor Short Form Are Required for Its Inhibitory Action on the Function of ... Mixed-Disulfide Folding Intermediates between Thyroglobulin and Endoplasmic Reticulum Resident Oxidoreductases ERp57 and ... Protein Disulfide Isomerase Bruno Di Jeso, Young-nam Park, Luca Ulianich, A. Sonia Treglia, Malene L. Urbanas, Stephen High, ...
PRNewswire/ -- Using optical and electrical measurements, a two-dimensional anisotropic crystal of rhenium disulfide was found ... Rhenium disulfide (ReS2) is a two-dimensional (2D) material crystallizing into a flake-like structure, as a black platelet ( ... Kanazawa University Research: Opposite Piezoresistant Effects of Rhenium Disulfide in two Principle Directions ... This novel finding is expected to lead to wide application of rhenium disulfide. ...
Methyl disulfide; Linear Formula: CH3SSCH3; Empirical Formula: C2H6S2; find related products, papers, technical documents, MSDS ... Dimethyl disulfide (DMDS) is an organic dialkyl disulfide. It is one of the odorous compounds found on the working face of ... Dimethyl disulfide (DMDS) may be used to derivatize alkenes for the determination of position of double bond by MS. It may also ... Nutrition Research, Organic Building Blocks, Phytochemicals by Plant (Food/Spice/Herb), Sulfides/Disulfides, Sulfur Compounds ...
  • A research team under the National Taiwan University (NTU) has discovered an optoelectronic application for molybdenum disulfide (MoS2), a 2-dimensional semiconductor material, according to the team. (digitimes.com)
  • Synthesis of poorly crystalline, randomly oriented rag-like structures of molybdenum disulfide has been reported starting from aqueous solutions of ammonium molybdate, and thioacetamide in presence of sodium dodecyl sulfate via calcination of the amorphous precipitates, obtained through acidification of the in situ generated intermediate of ammonium tetrathiomolybdate. (hindawi.com)
  • Molybdenum disulfide (MoS 2 ) is a hexagonal layer structured material. (hindawi.com)
  • Detailed Product Description MOLYBDENUM DISULFIDE MoS2 is an important material for the chemicals and lubricant industries. (tradekey.com)
  • Moly has used as catalysts, paint pigments, corrosion inhibitors, smoke and flame retardants, dry lubricant (molybdenum disulfide) on space vehicles and resistant to high loads and temperatures. (tradekey.com)
  • Atomically thin molybdenum disulfide (MoS 2 ) is a promising semiconductor material for integrated flexible electronics due to its excellent mechanical, optical and electronic properties. (nature.com)
  • Molybdenum disulfide bilayers with well-defined interlayer twist angle were constructed by stacking single-crystal monolayers. (nih.gov)
  • Researchers with the Lawrence Berkeley National Laboratory (Berkeley Lab) have recorded the first observations of a strong nonlinear optical resonance along the edges of a single layer of molybdenum disulfide. (phys.org)
  • The existence of these edge states is key to the use of molybdenum disulfide in nanoelectronics, as well as a catalyst for the hydrogen evolution reaction in fuel cells, desulfurization and other chemical reactions. (phys.org)
  • We observed strong nonlinear optical resonances at the edges of a two-dimensional crystal of molybdenum disulfide" says Xiang Zhang, a faculty scientist with Berkeley Lab's Materials Sciences Division who led this study. (phys.org)
  • For the SHG imaging of molybdenum disulfide, Zhang and his collaborators illuminated sample membranes that are only three atoms thick with ultrafast pulses of infrared light. (phys.org)
  • The paper is published in the journal Nature Communications ( 'Misorientation-angle-dependent electrical transport across molybdenum disulfide grain boundaries' ). (nanowerk.com)
  • This specification covers requirements for a lubricant consisting of molybdenum disulfide and isopropanol, intended for use with metal parts having limited clearances and in applications where control of impurities is required. (everyspec.com)
  • Engineer brings new twist to sodium ion battery technology with discovery of flexible molybdenum disulfide electrodes Gurpreet Singh, assistant professor of mechanical and nuclear engineerin. (innovationtoronto.com)
  • MIT researchers produce complex electronic circuits from molybdenum disulfide, a material that could have many more. (innovationtoronto.com)
  • This disulfide-locked dimeric assembly provides a new element of structural diversity for cysteine-rich peptides as well as increased protease resistance, broad-spectrum antimicrobial activity, and enhanced potency against the opportunistic human pathogen Acinetobacter baumannii. (nih.gov)
  • For example, researchers have identified several pairs of peptides that are unstructured in isolation, but adopt stable secondary and tertiary structure upon forming a disulfide bond between them. (wikidoc.org)
  • As a result, the denaturation of cyclic peptides can often be attributed to the stability of disulfide bonds. (wikibooks.org)
  • We offer Protein Disulfide Isomerase/P4HB Peptides and Protein Disulfide Isomerase/P4HB Proteins for use in common research applications: Blocking/Neutralizing, Control, ELISA, Protein Array, SDS-Page, Western Blot. (novusbio.com)
  • Our Protein Disulfide Isomerase/P4HB Peptides and Protein Disulfide Isomerase/P4HB Proteins can be used in a variety of model species: Human. (novusbio.com)
  • Choose from our Protein Disulfide Isomerase/P4HB Peptides and Proteins. (novusbio.com)
  • As a result, peptides containing disulfide bonds are often appealing for peptide pharmaceuticals making them an area of active research. (cem.com)
  • The microwave has enabled the high quality synthesis of longer 30-40 amino acid peptides with up to 4 disulfide bonds using multiple cysteine side chain protecting groups. (cem.com)
  • The disulfide bonds that form between two cysteine residues are important in defining and rigidifying the structures of proteins and peptides. (ebscohost.com)
  • Production of Recombinant Disulfide-Rich Venom Peptides for Structural and Functional Analysis via Expression in the Periplasm of E. coli Klint, Julie K. (ebscohost.com)
  • Disulfide-rich peptides are the dominant component of most animal venoms. (ebscohost.com)
  • Disulfide bond formed by two cysteine residues at C-terminus of frog skin peptides precludes one to determine sequence inside the forming loop. (diva-portal.org)
  • However, low-energy CID spectra of natural non-tryptic peptides with C-terminal disulfide cycle demonstrate an unusual fragmentation route, which may be used to elucidate the "hidden" C-terminal sequence. (diva-portal.org)
  • Potentides: Novel Cysteine-Rich Peptides with Unusual Disulfide Connectivity from Potentilla anserina. (bioportfolio.com)
  • Towards Structure Determination of Disulfide-Rich Peptides Using Chemical Shift-Based Methods. (bioportfolio.com)
  • Disulfide-rich peptides are a class of molecules for which NMR spectroscopy has been the primary tool for structural characterization. (bioportfolio.com)
  • Cyclic disulfide-bridged peptides can be prepared rapidly with good purity using microwave-enhanced SPPS on the Liberty Blue automated microwave peptide synthesizer. (cem.com)
  • This webinar recording demonstrates strategies to synthesize peptides containing one, two, or three disulfide bonds with regioselective control simplfied by the Initatior+ Alstra™ Branches™ software. (biotage.com)
  • Disulfide rich peptides (DRP) offer unique stability and plasticity when considering scaffolds for peptide-based therapeutics. (biotage.com)
  • While the linear synthesis of these peptides can be relatively straightforward, ensuring that the proper disulfide bond pattern is achieved reproducibly can be difficult but is absolutely critical for a successful discovery effort to proceed forward. (biotage.com)
  • Learn simplified strategies that enable automated and regioselective formation of disulfide bonds in peptides with complex folding patterns. (biotage.com)
  • Both peptides are useful inhibitors of TTX-sensitive voltage-gated sodium channels and are composed of six cysteine residues that form three disulfide bonds, respectively. (scielo.br)
  • Most venom peptides are highly bridged proteins with multipairs of intrachain disulfide bonds. (scielo.br)
  • Therefore, the understanding of disulfide linkage patterns is necessary for further studies relating structure to function of venom peptides (5-7). (scielo.br)
  • Therefore, the method presented in Figure 1 can be employed to identify the disulfide linkage pattern of venom peptides. (scielo.br)
  • Moreover, this study may also confirm that strategies employed herein are very consistent to assign disulfide bonds of venom peptides. (scielo.br)
  • Participates in the folding of proteins containing disulfide bonds, may be involved in glycosylation, prolyl hydroxylation and triglyceride transfer. (uniprot.org)
  • I am finding that my structures generated with VMD containing disulfide bonds are not being preserved when used in PyRosetta. (rosettacommons.org)
  • citation needed] Alternatively, disulfide bonds in proteins often formed by thiol-disulfide exchange: RS−SR + R′SH ⇌ R′S−SR + RSH Such reactions are mediated by enzymes in some cases and in other cases are under equilibrium control, especially in the presence of a catalytic amount of base. (wikipedia.org)
  • Disulfide bonds in proteins are formed between the thiol groups of cysteine residues. (wikidoc.org)
  • Disulfide bonds in proteins are formed by thiol-disulfide exchange reactions. (wikidoc.org)
  • The article characterizes disulfide bonds in proteins. (ebscohost.com)
  • n➝ π* Interactions Modulate the Properties of Cysteine Residues and Disulfide Bonds in Proteins. (bioportfolio.com)
  • The prototype of a protein disulfide bond is the two-amino-acid peptide, cystine , which is composed of two cysteine amino acids joined by a disulfide bond (shown in Figure 2 in its unionized form). (wikidoc.org)
  • Most cyclic peptide bonds are formed between disulfide bonds. (wikibooks.org)
  • Each Protein Disulfide Isomerase/P4HB Peptide and Protein Disulfide Isomerase/P4HB Protein is fully covered by our Guarantee+, to give you complete peace of mind and the support when you need it. (novusbio.com)
  • For example, the formation of disulfide bridges within the peptide will create 'protein folding' containing the carbon-14 label. (thefreedictionary.com)
  • This article describes a protocol for producing and purifying disulfide-stabilized transmembrane peptide complexes that are suitable for structural analysis by solution nuclear magnetic resonance (NMR) and other analytical applications. (jove.com)
  • This study demonstrates that UNIFI - a compliance-ready software - is designed to support biopharmaceutical laboratories in performing fast peptide mapping and monitoring of mAb disulfide linkages. (waters.com)
  • Finally, a peptide venom from cone snails containing two disulfide bridges (conotoxin-SI) was synthesized in under 4 h with 67% purity. (cem.com)
  • With the recent FDA approval of Linaclotide, a 14 amino acid peptide with three disulfide bonds for the treatment of Irritable Bowel Syndrome, exemplifies the utility of this peptide class. (biotage.com)
  • Peptide toxins are usually highly bridged proteins with multipairs of intrachain disulfide bonds. (scielo.br)
  • In this paper, we successfully assigned the disulfide linkage of two novel peptide toxins, called HNTX-III and HNTX-IV, isolated from the venom of Ornithoctonus hainana spider. (scielo.br)
  • In addition, this study also showed that this method may have a great potential for determining the disulfide bonds of spider peptide toxins. (scielo.br)
  • The traditional method for disulfide bond assignment consists of breaking the peptide chain with proteases and isolating bridged fragments. (scielo.br)
  • In addition, peptide cleavage is usually produced in basic solutions, which would result in ambiguities due to disulfide scrambling problems. (scielo.br)
  • First, the peptide was partially reduced by TCEP at pH 3.0 and separated by RP-HPLC, which yielded intermediates with intact disulfide bond/bonds and free thiols. (scielo.br)
  • In biology, disulfide bridges formed between thiol groups in two cysteine residues are an important component of the secondary and tertiary structure of proteins . (wikipedia.org)
  • Protein disulfide isomerase (PDI) is a multifunctional protein that facilitates the formation of correct disulfide crosslinks between cysteine residues during the early stages of protein folding and secretion in the endoplasmic reticulum. (els.net)
  • These results indicate that channel function is controlled by disulfide bond formation between intracellular residues on distinct ASIC1a subunits. (pnas.org)
  • 2) The disulfide bond may form the nucleus of a hydrophobic core of the folded protein, i.e., local hydrophobic residues may condense around the disulfide bond and onto each other through hydrophobic interactions . (wikidoc.org)
  • 3) Related to #1 and #2, the disulfide bond link two segments of the protein chain, the disulfide bond increases the effective local concentration of protein residues and lowers the effective local concentration of water molecules. (wikidoc.org)
  • Two cysteine residues can be linked by a disulfide bond to form cystine. (wikibooks.org)
  • If the protein's amino acid residues, specifically cysteines, are close to one another they will form a disulfide bond even if it is not properly folded. (wikibooks.org)
  • In polypeptides containing multiple cysteine residues, disulfide isomerization can lead to multiple products with different biological activities. (ebscohost.com)
  • The formation of correct disulfide bonds between cysteine residues ensures p. (bioportfolio.com)
  • They have six cysteine residues that constitute three disulfide bonds as revealed by matrix assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF MS) and sequence analysis (10, 11). (scielo.br)
  • PDIs help non-native disulfides become native disulfides by acting as a catalyst to the isomerization process (they have to help brake the non-native disulfide bond so that the protein can finish folding properly before they can form the native disulfide bond) (Figure 1). (wikibooks.org)
  • Dsb proteins (DsbA, DsbB, DsbC, and DsbD) catalyze formation and isomerization of protein disulfide bonds in the periplasm of Escherichia coli. (prospecbio.com)
  • Randomly reoxidized soybean trypsin-inhibitor and possibility of conformational barriers to disulfide isomerization in proteins. (springer.com)
  • Genetic and biochemical experiments show that, when released from the bilayer, Lyz is activated by an intramolecular thiol-disulfide isomerization, which requires a cysteine in its N-terminal SAR (signal-arrest-release) domain. (sciencemag.org)
  • Native disulfide bond formation in protein-biosynthesis - Evidence for the role of protein disulfide isomerase. (springer.com)
  • The following resources provide information about occupational exposure to carbon disulfide. (cdc.gov)
  • Natural Advantage introduces natural Bis(2-methyl-3-furyl) disulfide (FEMA# 3259, CAS# 28588-75-2). (perfumerflavorist.com)
  • Although typically used for meats, bis(2-methyl-3-furyl) disulfide can also be used to add fatty notes to material as well as add creamy and milky effects at low dosage. (perfumerflavorist.com)
  • in contrast, the high-molecular-weight glutenins are formed by disulfide linkages of several diverse polypeptide chains which have been separated and characterized. (springer.com)
  • Most of the cross-linkages are from disulfide bonds formed by the oxidation of two cysteine amino acids. (wikibooks.org)
  • Crystal structures confirm the alternative disulfide linkages in the two forms of Lyz and reveal dramatic conformational differences in the catalytic domain. (sciencemag.org)
  • 4,5 This approach provides biopharmaceutical laboratories with a compliance-ready tool for fast mapping and monitoring of the disulfide linkages of mAbs. (waters.com)
  • By using the strategy above, disulfide linkages of HNTX-III and HNTX-IV were determined as I-IV, II-V and III-VI pattern. (scielo.br)
  • The determination of disulfide linkages of both toxins may help to interpret their structure and function. (scielo.br)
  • Benham AM. The protein disulfide isomerase family: key players in health and disease. (springer.com)
  • Identification of the protein disulfide isomerase family member PDIp in experimental Parkinson's disease and Lewy body pathology. (springer.com)
  • The amount of carbon disulfide released into the air through natural processes is difficult to judge because it is so small. (cdc.gov)
  • myst32YT mas also made a small amount of carbon disulfide. (sciencemadness.org)
  • How might I be exposed to carbon disulfide? (cdc.gov)
  • The people most often exposed to carbon disulfide are workers in plants that use carbon disulfide in their manufacturing processes. (cdc.gov)
  • Is there a medical test to show whether I've been exposed to carbon disulfide? (cdc.gov)
  • Winkelmann J. (2018) Diffusion coefficient of hexane in carbon disulfide. (springer.com)
  • Strong light-matter interaction in tungsten disulfide nanotubes, Physical Chemistry Chemical Physics (2018). (phys.org)
  • Formamidine disulfide dihydrochloride (CAS 14807-75-1) Market Research Report 2018 aims at providing comprehensive data on formamidine disulfide dihydrochloride market globally and regionally (Europe, Asia, North America, Latin America etc. (marketpublishers.com)
  • Formamidine disulfide dihydrochloride (CAS 14807-75-1) Market Research Report 2018 contents were worked out and placed on the website in March, 2018. (marketpublishers.com)
  • Please note that Formamidine disulfide dihydrochloride (CAS 14807-75-1) Market Research Report 2018 is a half ready publication and contents are subject to change. (marketpublishers.com)
  • 260-132 8 Claims ABSTRACT OF THE DISCLOSURE An ashless dispersant for lubricants which is made by reacting carbon disulfide or carbon disulfide and an alkali metal hydroxide with a Mannich condensation product. (google.es)
  • In chemistry , a disulfide refers to a functional group with the structure R− S−S −R′. The linkage is also called an SS-bond or sometimes a disulfide bridge and is usually derived by the coupling of two thiol groups. (wikipedia.org)
  • The disulfide bonds are strong, with a typical bond dissociation energy of 60 kcal/mol (251 kJ mol −1 ). (wikipedia.org)
  • However, being about 40% weaker than C−C and C−H bonds , the disulfide bond is often the "weak link" in many molecules. (wikipedia.org)
  • The disulfide bond is about 2.05 Å in length, about 0.5 Å longer than a C−C bond. (wikipedia.org)
  • Furthermore, reflecting the polarizability of divalent sulfur, the S−S bond is susceptible to scission by polar reagents, both electrophiles and especially nucleophiles (Nu): RS−SR + Nu− → RS−Nu + RS− The disulfide bond is about 2.05 Å in length, about 0.5 Å longer than a C−C bond. (wikipedia.org)
  • Tetrakis(2-methylpropyl)thioperoxydicarbonic diamide, or tetraisobutylthiuram disulfide, C18H36N2S4, crystallizes in a general position in the triclinic space group P-1 but shows pseudo-C2 symmetry about the disulfide bond. (ingentaconnect.com)
  • Hatahet F and Ruddock LW (2009) Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation. (els.net)
  • Cys-495 in the ASIC1a C terminus was particularly important for inter-subunit disulfide bond formation, although other C-terminal cysteines contributed. (pnas.org)
  • Inter-subunit disulfide bond formation reduced the proportion of ASIC1a located on the cell surface and contributed to the H 2 O 2 -induced decrease in H + -gated current. (pnas.org)
  • ASIC1a has many conserved cysteines that could be targets for disulfide bond formation, yet it is unknown if oxidants affect those cysteines to alter ASIC1a structure. (pnas.org)
  • We discovered that oxidation enhances disulfide bond formation between ASIC1a subunits. (pnas.org)
  • Dimethyl disulfide (DMDS) may be used to derivatize alkenes for the determination of position of double bond by MS. It may also be used to determine the location of the double-bond position of monounsaturated fatty acids in Campylobacter cryaerophila by combined GC-MS analysis. (sigmaaldrich.com)
  • Intermolecular disulfide bond to modulate protein function as a redox-sensing switch. (nih.gov)
  • In chemistry , a disulfide bond is a single covalent bond derived from the coupling of thiol groups. (wikidoc.org)
  • The linkage is also called an SS-bond or disulfide bridge. (wikidoc.org)
  • Figure 1: Formal depiction of disulfide bond formation as an oxidation. (wikidoc.org)
  • Cystine is composed of two cysteines linked by a disulfide bond (shown here in its neutral form). (wikidoc.org)
  • A disulfide bond is typically denoted by hyphenating the abbreviations for cysteine, e.g., the "Cys26-Cys84 disulfide bond", or the "26-84 disulfide bond", or most simply as "C26-C84" where the disulfide bond is understood and does not need to be mentioned. (wikidoc.org)
  • The disulfide bond stabilizes the folded form of a protein in several ways: 1) It holds two portions of the protein together, biasing the protein towards the folded topology. (wikidoc.org)
  • Expressed differently, the disulfide bond destabilizes the unfolded form of the protein by lowering its entropy . (wikidoc.org)
  • Since water molecules attack amide-amide hydrogen bonds and break up secondary structure , a disulfide bond stabilizes secondary structure in its vicinity. (wikidoc.org)
  • A disulfide bond , also called an S-S bond, or disulfide bridge, is a covalent bond derived from two thiol groups. (wikibooks.org)
  • The result is a disulfide bond called cystine connecting the polypeptide chains. (wikibooks.org)
  • The typical bond dissociation energy of a disulfide bond ranks at 60 kcal/mole and has a bond length of 2.05 Å. (wikibooks.org)
  • If a disulfide bond forms when the protein is not properly folded, they call this a non-native disulfide. (wikibooks.org)
  • Disulfide-Bond Isomerase Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 216 amino acids (21-236) and having a molecular mass of 23.5 kDa. (prospecbio.com)
  • In nature a large amount of proteins contain at least one disulfide bond. (cem.com)
  • Dr. Olga Avrutina has been actively researching synthetic improvements for oxidative folding through disulfide bond formation. (cem.com)
  • 13C NMR chemical shifts can predict disulfide bond formation. (ebscohost.com)
  • In this study we demonstrate that 13C NMR chemical shifts are diagnostic of disulfide bond formation, and can discriminate between cysteine in the. (ebscohost.com)
  • CD44 Binding to Hyaluronic Acid Is Redox Regulated by a Labile Disulfide Bond in the Hyaluronic Acid Binding Site. (ebscohost.com)
  • The observed cleavages may be quite competitive, revealing the sequence inside disulfide cycle, although S-S bond rupture does not occur in this case. (diva-portal.org)
  • In this application note, we describe a streamlined disulfide bond mapping analysis workflow using the Waters Biopharmaceutical Platform Solution with UNIFI. (waters.com)
  • This application note describes a UPLC-MS E analysis of monoclonal antibody (mAb) disulfide bond mapping using the Waters Biopharmaceutical Platform Solution with UNIFI. (waters.com)
  • Disulfide bond formation is critical for the structure, stability, and biological functions of therapeutic proteins. (waters.com)
  • 1 Disulfide bond linkage assignment, localization, and monitoring are therefore of great importance to ensure process consistency and product integrity during biotherapeutic drug development. (waters.com)
  • As shown in Figure 1, this workflow was used for the disulfide bond mapping analysis of the Waters Intact mAb Mass Check Standard, and for three batches each of infliximab innovator and biosimilar samples. (waters.com)
  • Disulfide bond mapping using the Waters Biopharmaceutical Platform Solution with UNIFI. (waters.com)
  • Most disulfides encountered in organo sulfur chemistry are symmetrical disulfides. (wikipedia.org)
  • In the converse reaction, carbanionic reagents react with elemental sulfur to afford mixtures of the thioether, disulfide, and higher polysulfides. (wikipedia.org)
  • Commercial carbon disulfide is made by combining carbon and sulfur at very high temperatures. (cdc.gov)
  • Hydrogen disulfide readily decomposes under ambient conditions to hydrogen sulfide and sulfur. (wikipedia.org)
  • The other sulfur-containing amino acid, methionine , cannot form disulfide bonds. (wikidoc.org)
  • The first method, involves the reaction of [[sulfur]] vapors with carbon (or coke, anthracite, or any other coal) at 900°C. The resulting vapors are condensed and sulfur disulfide is purified. (sciencemadness.org)
  • When biochemists want to break disulfide bonds within or between molecules, they add dithiothreitol to their buffer solutions. (acs.org)
  • However, the test is not specific for carbon disulfide exposure. (cdc.gov)
  • 1990. Carbon disulfide exposure and neurotoxic sequelae among viscose rayon workers. (cdc.gov)
  • If you believe you have become ill because of Carbon Disulfide exposure you should consider hiring a personal injury attorney. (legalmatch.com)
  • Tungsten Disulfide Nanoparticle Dispersions are suspensions of tungsten disulfide nanoparticles in water or various organic solvents such as ethanol or mineral oil. (americanelements.com)
  • In the laboratory, iodine in the presence of base is commonly employed to oxidize thiols to disulfides. (wikipedia.org)
  • Reagents that deliver the equivalent of "RS+" react with thiols to give asymmetrical disulfides: RSH + R′SNR″2 → RS−SR′ + HNR″2 where R″2N is the phthalimido group. (wikipedia.org)
  • In organosulfur chemistry, hydrogen disulfide adds to alkenes to give disulfides and thiols. (wikipedia.org)
  • It is a member of a large family of oxidoreductases that catalyse exchange reactions between thiols and disulfides. (els.net)
  • Partial reduction to create a series of intermediates containing both disulfides and thiols has been widely used in assignment of disulfide bonds. (scielo.br)
  • Moreover, the knowledge on such nontrivial optical features of these nanostructures sheds light on the possible light-harvesting properties of the nanocomposites based on disulfide nanotubes and plasmonic nanoparticles (gold or silver) which are extensively developed by young scientists from Faculty of Materials Science, MSU," said Alexander Polyakov, the co-author of the article. (phys.org)
  • Disulfide bonds are usually formed from the oxidation of sulfhydryl (−SH) groups , especially in biological contexts. (wikipedia.org)
  • Disulfide bonds are usually formed from the oxidation of sulfhydryl (-SH) groups , as depicted formally in Figure 1. (wikidoc.org)
  • However, regiospecific disulfide bonding based on standard post-synthetic oxidation methods present significant synthetic challenges. (cem.com)
  • In addition to the classic NO-cGMP pathway, PKG can also be activated by an oxidation mechanism during which the homodimer complex forms an interprotein disulfide. (ahajournals.org)
  • 5 The disulfide forms in the N-terminus of PKG1α, which is held together by a leucine zipper, with structural studies confirming that Cys42 on each chain closely aligns to explain the susceptibility to oxidation. (ahajournals.org)
  • The catalysis of disulfide formation relies almost entirely on the high reactivity of PDI's active site disulfides. (els.net)
  • The kinetically influential ionizations of caricain D158N revealed by using 4,4'-dipyrimidyl disulfide as a reactivity probe. (semanticscholar.org)
  • Although the hydrogenation of disulfides is usually not practical, the equilibrium constant for the reaction provides a measure of the standard redox potential for disulfides: RSSR + H2 → 2 RSH This value is about −250 mV versus the standard hydrogen electrode (pH = 7). (wikipedia.org)
  • Reducing equivalents, to help balance the redox state and allow disulfide isomerisation are introduced from the cytoplasm by translocation of the newly synthesises substrate and by a glutathione ( GSH )‐dependent mechanism. (els.net)
  • Disulfides increase the stability of the protein and also "regulate redox-dependent functions," and over the years, our ideas of how disulfides form in proteins have drastically changed. (wikibooks.org)
  • the interaction retains P4HB at the cell surface of Th2 T helper cells, increasing disulfide reductase activity at the plasma membrane, altering the plasma membrane redox state and enhancing cell migration. (uniprot.org)
  • Galectin-9 binding to cell surface protein disulfide isomerase regulates the redox environment to enhance T-cell migration and HIV entry. (springer.com)
  • Disulfides where the two R groups are the same are called symmetric, examples being diphenyl disulfide and dimethyl disulfide . (wikipedia.org)
  • Protein kinase G (PKG) is activated by nitric oxide (NO)-induced cGMP binding or alternatively by oxidant-induced interprotein disulfide formation. (ahajournals.org)
  • The gliadin proteins contain mostly intramolecular disulfide bonds. (springer.com)
  • Intermolecular disulfide bonds occur between polypeptide chains while intramolecular disulfide bonds occur within a polypeptide chain and are usually responsible for stabilizing tertiary structures of proteins. (wikibooks.org)
  • Disulfide bonds play an important role in the folding and stability of some proteins, usually proteins secreted to the extracellular medium. (wikidoc.org)
  • Extracellular proteins often have several disulfide bonds, whereas intracellular proteins usually lack them. (wikibooks.org)
  • 2015) Extracellular disulfide bridges stabilize TRPC5 dimerization, trafficking, and activity. (thefreedictionary.com)
  • Hydrogen disulfide is the inorganic compound with the formula H2S2. (wikipedia.org)
  • The structure of hydrogen disulfide is similar to that of hydrogen peroxide, with C2 point group symmetry. (wikipedia.org)
  • Hydrogen disulfide can be synthesised by dissolving alkali metal or alkaline earth metal polysulfides in water. (wikipedia.org)
  • Fractional distillation of this oil gives hydrogen disulfide separate from any other polysulfides (mostly trisulfide). (wikipedia.org)
  • The deuterated form of hydrogen disulfide DSSD, has a similar geometry to HSSH, but its tunneling time is slower, making it a convenient test case for the quantum Zeno effect, in which frequent observation of a quantum system suppresses its normal evolution. (wikipedia.org)
  • Two-dimensional metallic tantalum disulfide as a hydrogen evolution catalyst. (nature.com)
  • Facile synthesis of single crystal vanadium disulfide nanosheets by chemical vapor deposition for efficient hydrogen evolution reaction. (nature.com)
  • More particularly, the invention relates to the production of C 4 products by the interaction of methanol, hydrogen and carbon monoxide in the presence of a cobalt catalyst, an iodine promoter and a biphosphine disulfide component wherein the molar ratio of cobalt to phosphorus components can be controlled to provide a catalyst system highly selective to the production of C 4 products. (google.com)
  • Symmetrical disulfides are compounds of the formula R 2 S 2 . (wikipedia.org)
  • [4] Selenium disulfide is an inorganic compound with the chemical formula SeS 2 . (wikipedia.org)
  • In inorganic chemistry disulfide usually refers to the corresponding anion S2− 2 (−S−S−). A selection of disulfides Symmetrical disulfides are compounds of the formula R2S2. (wikipedia.org)
  • When the angle approaches 0° or 180°, then the disulfide is a significantly better oxidant. (wikipedia.org)
  • We found that ASIC1a formed inter-subunit disulfide bonds and the oxidant H 2 O 2 increased this link between subunits. (pnas.org)
  • Mechanistically, this is explained by loss of cGMP allowing disulfide formation in response to basal oxidant production. (ahajournals.org)
  • In organic synthesis, hydride agents are typically employed for scission of disulfides, such as sodium borohydride. (wikipedia.org)
  • A useful search term for carbon disulfide includes "carbon bisulfide," "carbon sulfide," and "carbon disulphide. (cdc.gov)
  • The amounts of reactants may vary, but in general, about 0.25 to 3.0 moles of carbon disulfide are contracted with about 1 equivalent weight of the Mannich product (one equivalent weight of the Mannich product being the molecular Weight of the Mannich product divided by the number of reactive nitrogen atoms present per molecule). (google.es)
  • An analysis of the molecular dynamics (МD) of the interaction between a carbon nanotube (CNT) and a carbon disulfide active solvent (CS2) has been carried out. (scirp.org)
  • Kholmurodov, K. , Aru, G. and Yasuoka, K. (2010) Molecular dynamics simulations of the interaction of carbon nanotube and a carbon disulfide solvent. (scirp.org)
  • Aksenov, V.L., Avdeev, M.V. and Kholmurodov, Kh.T. (2007) Organization of solvent at interface with fullerene in solution C60/carbon disulfide by molecular bynamics simulations. (scirp.org)
  • They are less common in organic chemistry, but most disulfides in nature are unsymmetrical. (wikipedia.org)
  • I want to get the latest chemistry news from C&EN in my inbox every week. (acs.org)
  • The ability to form disulfides between cysteines in substrate proteins results from highly reactive active site disulfides. (els.net)
  • In proteins with more than two cysteines, non-native disulfide species may be formed, which are almost always unfolded. (wikidoc.org)
  • The alkylation of alkali metal di- and polysulfides gives disulfides. (wikipedia.org)
  • SUMMARY OF THE INVENTION We have discovered novel dispersants which are formed by reacting carbon disulfide or carbon disulfide and an alkali metal hydroxide with a Mannich condensation product. (google.es)
  • Both types react with carbon disulfide or carbon disulfide and an alkali metal hydroxide to produce excellent dispersants. (google.es)
  • When carbon disulfide and the alkali metal hyroxide are used, the ratio by weight of carbon disulfide to the hydroxide ranges from about 2:1 to 1:2, preferably 1:1. (google.es)
  • It is well known that disulfide bonds confer conformational stability to folded proteins. (scielo.br)
  • The most important aspect of disulfide bonds is their cleavage, which occurs via reduction. (wikipedia.org)
  • Bunte salts, derivatives of the type RSSO3-Na+ are also used to generate unsymmetrical disulfides: Na[O3S2R] + NaSR' → RSSR' + Na2SO3 The most important aspect of disulfide bonds is their cleavage, which occurs via reduction. (wikipedia.org)
  • Cleavage of disulfide bonds of wheat glutenin by mercuric chloride. (springer.com)
  • Enzymatic post translational cleavage of labile disulfide bonds is a mechanism by which proteins are structurally regulated by imparting an allosteric change and altering. (ebscohost.com)
  • Tetraisobutylthiuram disulfide molecules of one optical configuration form sheets in the plane of the a and b axes. (ingentaconnect.com)
  • She said, 'It helps in stiffening of outer dense fibers by formation of disulfide bridges or strong bonding protein molecules during sperm maturation, which is an essential step for generation of sperm motility, especially progressive motility as shown in the study. (thefreedictionary.com)
  • Carbon disulfide (CS 2 ) is a colorless liquid with an ether-like odor. (cdc.gov)
  • Pure carbon disulfide is a colorless liquid with a pleasant odor that is like the smell of chloroform. (cdc.gov)
  • Physical=== Carbon disulfide is a colorless liquid, with an chloroform like smell when pure. (sciencemadness.org)
  • In the cell, PDI's essential activity is the formation of disulfide bonds, but it does catalyse isomerisation. (els.net)
  • A high degree of selectivity towards the formation of butanol and butanal is provided by using the cobalt entity and the biphosphine disulfide in a molar ratio in the range of about 2:1 to about 10:1, based on elemental cobalt and phosphorus. (google.com)
  • In the journal article "Multiple ways to make disulfides" by Neil J. Bulleid and Lars Ellgaard, they discuss how disulfides can be formed in the endoplasmic reticulum (ER), and the different enzymes that catalyze the pathways of formation. (wikibooks.org)
  • This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. (uniprot.org)
  • In summary, cGMP binding to PKG induces a state that is resistant to disulfide formation. (ahajournals.org)
  • A nontrivial observation for the CNTCS2 system is that the solvent carbon disulfide atoms make up a patterned (layered) formation around the carbon nanotube. (scirp.org)
  • On the other hand, intermolecular disulfide bonds are attributed to stabilizing quaternary protein structures. (wikibooks.org)
  • Many specialized methods have been developed for forming unsymmetrical disulfides. (wikipedia.org)
  • Immediately Dangerous to Life or Health Concentrations (IDLH) of Carbon Disulfide -NIOSH reviews relevant scientific data and researches methods for developing IDLH values. (cdc.gov)
  • The present invention also relates to DNA sequences encoding the protein disulfide isomerases, compositions comprising said protein disulfide isomerases and methods of use thereof. (patentgenius.com)
  • The presence of disulfide bonds can be detected unambiguously only by X-ray crystallography, and otherwise must be inferred by chemical methods. (ebscohost.com)
  • The report includes formamidine disulfide dihydrochloride description, covers its application areas, manufacturing methods, patents. (marketpublishers.com)
  • Rate constants for the reaction of hydroxyl radicals with carbonyl sulfide, carbon disulfide and dimethyl thioether over the temperature range 299-430 K. (cdc.gov)
  • Catalysis of the reaction: 2 glutathione + NADP+ = glutathione disulfide + NADPH + H+. (yeastgenome.org)
  • This patent portrays a need for improved dispersants, and disclose dispersants formed by the reaction between an alklylene polyamine, carbon disulfide, and a hydrocarbon substituted dicarboxylic acid. (google.es)
  • The reaction between disulfides and phosphines generates a reversible disulfide metathesis process. (diva-portal.org)
  • Exposure to carbon disulfide can occur by breathing it in the air and by drinking water or eating foods that contain it. (cdc.gov)
  • 1988. Neurological examination, computerized- tomography, cerebral blood-flow and neuropsychological examination in workers with long-term exposure to carbon disulfide. (cdc.gov)
  • 1992. Regional cerebral blood flow after long-term exposure to carbon disulfide. (cdc.gov)
  • The exposure under study was carbon disulfide, a chemical used in rubber chemicals department. (cdc.gov)
  • Risks - Short-term exposure to carbon disulfide can result in headache, dizziness, fatigue and nausea. (legalmatch.com)
  • NIOSHTIC-2 search results on carbon disulfide -NIOSHTIC-2 is a searchable database of worker safety and health publications, documents, grant reports, and journal articles supported in whole or in part by NIOSH. (cdc.gov)
  • Carbon Disulfide: Rubber and Plastics Chemical Manufacturing -The NIOSH Worker Notification Program notifies workers and other stakeholders about the findings of these research studies. (cdc.gov)
  • DHHS (NIOSH) Publication No. 77-156 (1977)-This report increases awareness and recommends work practices to reduce exposures to carbon disulfide in the workplace. (cdc.gov)
  • Catalysis of disulfide isomerisation. (els.net)