• While CXC disulfide bonds were found sterically unfavorable, CXXC were favored over longer-range disulfide bonds along the peptide backbone, in line with the high abundance of CXXC motifs in redox proteins. (rsc.org)
  • DsbA, a monomeric 21-kDa periplasmic protein, plays an important role in the folding of cell envelope proteins by catalyzing disulfide bond formation using a catalytic CXXC motif (for a review, see reference 35 ). (asm.org)
  • 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. (caltech.edu)
  • 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)
  • 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 bond formation is a crucial step in the folding of numerous cell-surface proteins. (nii.ac.jp)
  • Using the system, we found that isomerization of nonnative disulfides to native ones, a key step in the folding of many cell-surface proteins, takes place at a specific timing during synthesis in a manner dependent of a downstream region of the polypeptide. (nii.ac.jp)
  • This gene encodes a member of the disulfide isomerase (PDI) family of endoplasmic reticulum (ER) proteins that catalyze protein folding and thiol-disulfide interchange reactions. (nih.gov)
  • Mixed disulfides between glutathione and the reduced forms of disulfide-bonded proteins were generated and characterized to explore their suitability as models of the unfolded state of newly-synthesized secretory proteins. (kent.ac.uk)
  • The results indicate that these GS-S-protein mixed disulfide derivatives are ideal model unfolded proteins that can be used as substrates for detailed studies on secretory protein folding in vitro and on the interactions between unfolded proteins and facilitators of protein folding. (kent.ac.uk)
  • Considering that disulfide bonds will only form between optimally placed Cys in the tertiary structure, it follows that these bonds are a relatively recent addition to proteins. (biomedcentral.com)
  • The catalytic bonds are typically at the active sites of enzymes that mediate thiol/disulfide exchange in other proteins. (biomedcentral.com)
  • Bacterial D i s ulfide b ond forming (Dsb) proteins facilitate proper folding and disulfide bond formation of periplasmic and secreted proteins. (biomedcentral.com)
  • Guanylylation-competent replication proteins of Tomato mosaic virus are disulfide-linked. (jove.com)
  • Disulfide bridges are an important structural element in many proteins and peptides. (iris-biotech.de)
  • The secretory pathway contains oxidative systems which introduce disulfides into proteins for transport. (nanotempertech.com)
  • The extra disulfide bridge extends between residues 80 and 171, thus joining the variable and constant domains. (jimmunol.org)
  • 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. (jimmunol.org)
  • The basis of our approach is the use of disulfide cross-linking to identify residues that are within close proximity. (caltech.edu)
  • Circular dichroism spectra show that the zipper domains remain helical after cysteine residues and disulfide bonds are introduced. (caltech.edu)
  • Asymmetric placement of the cysteine residues in the leucine zipper domains suppresses intramolecular disulfide bonds and creates linked "multichains" composed of ca. 9 protein chains on average, as determined by multiangle light scattering measurements. (caltech.edu)
  • 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)
  • The thiol-disulfide exchange reaction in model systems and small peptides was investigated by means of a combined QM/MM metadynamics scheme. (rsc.org)
  • The structure of the transition state as well as the free energy barrier were very similar for the intramolecular thiol-disulfide reactions in model peptides. (rsc.org)
  • 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. (jimmunol.org)
  • These peptides were assembled and activated through disulfide bridge formation with complementary oligo-arginines containing an N-terminal cysteine residue. (rsc.org)
  • Although we demonstrated that activation of short oligo-arginine peptides is possible by extension of their sequence, its dependency on the formation of disulfide bridges hampers their use for in situ activation due to the dominant oxidative environment and the presence of potentially interfering thiols in many cellular environments. (rsc.org)
  • This brochure is a guideline how to plan and execute the synthesis of peptides with one or several disulfide bridges. (iris-biotech.de)
  • Here, we report that selective breakage of two conserved disulfide bonds located at the knees of integrin α 4 C589-C594 and β 7 C494-C526 activated α 4 β 7 . (biologists.org)
  • 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. (jimmunol.org)
  • It is a single polypeptide chain with one free sulfhydryl group (Cys34) and 17 intrachain disulfide bonds. (mpbio.com)
  • 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)
  • Most disulfides encountered in organo sulfur chemistry are symmetrical disulfides. (wikipedia.org)
  • The disulfides are treated as symmetrical. (biomedcentral.com)
  • The six in the growth hormone binding domain form disulfide bonds, and help the receptor to gain its correct three-dimensional structure. (biologists.org)
  • They form disulfide bonds as indicated: C38-C48 connects neighbouring strands A and B of the three-stranded sheet (bond 1). (biologists.org)
  • Interactions between the four membrane-spanning stretches of the Tar dimer were probed by measuring the tendency of 48 cysteine substitutions throughout this region to form disulfide cross-links with one another. (caltech.edu)
  • Both a and a domains contains an active site with the sequence motif -Cys-Gly-His-Cys-involved directly in thiol-disulfide exchange reactions. (rcsb.org)
  • Structural comparison of the PDI b domain with thioredoxin and PDI a reveals several features important for thiol-disulfide exchange activity. (rcsb.org)
  • The self-healing mechanism is not related to disulfide - disulfide exchange reactions, but to thiol - disulfide exchange reactions that are pH-dependent. (rsc.org)
  • Journal Article] Methods to identify the substrates of thiol-disulfide oxidoreductases. (nii.ac.jp)
  • A general feature of thiol-disulfide exchange reactions is the need to avoid a long lived product complex between protein partners. (ox.ac.uk)
  • The HIV envelope glycoprotein gp120, for example, is regulated by thiol/disulfide exchange and contains allosteric -RHStaple bonds that can exist in the -LHStaple configuration. (biomedcentral.com)
  • The WFDC domain, or WAP signature motif, contains eight cysteines forming four disulfide bonds at the core of the protein, and functions as a protease inhibitor. (nih.gov)
  • The X-ray crystal structure of Mt-DsbA reveals a two-domain structure, comprising a canonical thioredoxin domain with the conserved CXXC active site cysteines in their reduced form, and an inserted α-helical domain containing a structural disulfide bond. (biomedcentral.com)
  • At pH 5-7 it contains 17 intrachain disulfide bridges and 1 sulfhydryl group. (mpbio.com)
  • Disulfide bridges remain intact while native insulin converts into amyloid fibrils. (jove.com)
  • I didn't even use oxidative environment to trigger disulfide bond formation. (protocol-online.org)
  • These findings provide a number of new insights into the disulfide bond formation system of mammalian cells. (nii.ac.jp)
  • By using chemical reduction techniques and nuclear magnetic resonance (NMR), this increased molecular weight was due to disulfide bond formation as well as general oxidation and ester formation. (usda.gov)
  • With each pass, the molecular weight of the zein increased due to disulfide bond formation. (usda.gov)
  • [4] Selenium disulfide is an inorganic compound with the chemical formula SeS 2 . (wikipedia.org)
  • Hydrogen disulfide is the inorganic compound with the formula H2S2. (wikipedia.org)
  • So you suspect the dimer I got is not a proof for disulfide bond? (protocol-online.org)
  • Meanwhile, PEDV nsp9 is distinguished by the presence of a disulfide bond in the dimer interface. (nanotempertech.com)
  • Fibronectin is a large glycoprotein (220 kDa) composed of two polypeptide chains (dimer) joined by disulfide bonds at one end. (sigmaaldrich.com)
  • Disulfide bonds are usually formed from the oxidation of sulfhydryl (−SH) groups, especially in biological contexts. (wikipedia.org)
  • Oxidation state-dependent protein-protein interactions in disulfide cascades. (ox.ac.uk)
  • Intermolecular disulfide bond to modulate protein function as a redox-sensing switch. (nih.gov)
  • With one or two exceptions all the catalytic disulfides are +/-RHHooks, while the known allosteric disulfides are -RHStaples [ 8 ]. (biomedcentral.com)
  • 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)
  • The following stress conditions were applied for 15 min: heat shock at 50°C, cold shock at 10°C, disulfide stress caused by 2 or 10 mM diamide, oxidative stress caused by 1% hydrogen peroxide, salt stress caused by 1 M NaCl, and alcohol stress caused by 10% ethanol. (asm.org)
  • The stress conditions were heat shock at 50°C, cold shock at 10°C, disulfide stress caused by 2 mM diamide, oxidative stress caused by 1% hydrogen peroxide, salt stress caused by 1 M NaCl, and alcohol stress caused by 10% ethanol. (asm.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)
  • In organosulfur chemistry, hydrogen disulfide adds to alkenes to give disulfides and thiols. (wikipedia.org)
  • Protein disulfide isomerase (PDI) is a multifunctional protein of the endoplasmic reticulum, which catalyzes the formation, breakage and rearrangement of disulfide bonds during protein folding. (rcsb.org)
  • Moreover, on the substrates tested in this study, Mt-DsbA has disulfide bond isomerase activity contrary to Mt-DsbE and Mt-DsbF. (biomedcentral.com)
  • Dimerization results from intermonomer disulfide exchange between the canonical α-defensin Cys(II)-Cys(IV) (Cys(5)-Cys(20)) bonds located at the hydrophobic interface. (nih.gov)
  • Assembly and routing of von Willebrand factor variants: the requirements for disulfide-linked dimerization reside within the carboxy-terminal 151 amino acids. (rupress.org)
  • 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. (wakehealth.edu)
  • 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)
  • They are less common in organic chemistry, but most disulfides in nature are unsymmetrical. (wikipedia.org)
  • 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)
  • In an attempt to identify a common structural motif for allosteric disulfides the geometry and strain of 6,874 unique disulfide bonds in X-ray structures was recently examined [ 8 ]. (biomedcentral.com)
  • The spirals are the main structural disulfides. (biomedcentral.com)
  • Protein disulfide bonds can serve structural roles, and thus are often buried in the core of a protein. (biomedcentral.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)
  • Previous work suggested a role for DsbA, a periplasmic disulfide bond oxidase, in SPI1 T3SS function. (asm.org)
  • In a series of Crp4 disulfide variants whose cysteine connectivities were confirmed using NMR spectroscopy and mass spectrometry, mutagenesis did not induce loss of function. (nih.gov)
  • We then tested which positions support formation of a disulfide bond with a cysteine on a translocating polypeptide in the channel. (rupress.org)
  • Engineering of a cysteine residue into each leucine zipper domain allows formation of disulfide bonds templated by leucine zipper aggregation. (caltech.edu)
  • 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. (ox.ac.uk)
  • The alkylation of alkali metal di- and polysulfides gives disulfides. (wikipedia.org)
  • Hydrogen disulfide can be synthesised by dissolving alkali metal or alkaline earth metal polysulfides in water. (wikipedia.org)
  • To the contrary, the in vitro bactericidal activities of several Crp4 disulfide variants were equivalent to or greater than those of native Crp4. (nih.gov)
  • Although native Crp4 and the alpha-defensin moiety of proCrp4 resisted proteolysis completely, all disulfide variants were degraded extensively by MMP-7. (nih.gov)
  • By introducing a single cysteine at various positions in Escherichia coli SecY and testing its ability to form a disulfide bond with a single cysteine in a translocating chain, we provide evidence that translocating polypeptides pass through the center of the SecY complex. (rupress.org)
  • In the converse reaction, carbanionic reagents react with elemental sulfur to afford mixtures of the thioether, disulfide, and higher polysulfides. (wikipedia.org)
  • Fractional distillation of this oil gives hydrogen disulfide separate from any other polysulfides (mostly trisulfide). (wikipedia.org)
  • When the two R groups are not identical, the compound is said to be an asymmetric or mixed disulfide. (wikipedia.org)
  • The Disulfide bond is the one type of covalent bond that can play an important role in maintaining the tertiary structure as well as connecting two or more peptide chains together. (proteopedia.org)
  • 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. (ncl.ac.uk)
  • The middle disulfide-bond, C83-C94, is important for ligand binding. (biologists.org)
  • When two or all disulfide bonds are changed, ligand binding and activation are blocked. (biologists.org)
  • Hydrogen disulfide readily decomposes under ambient conditions to hydrogen sulfide and sulfur. (wikipedia.org)
  • Our results suggest that the disulfide loop in SEA contributes to toxin avidity for the TCR, rather than specificity for particular V beta. (jimmunol.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)
  • Mutation of the disulfide loop in staphylococcal enterotoxin A. Consequences for T cell recognition. (jimmunol.org)
  • This gene encodes a member of the WAP-type four-disulfide core (WFDC) domain family. (nih.gov)
  • The systematic name of this enzyme class is glutathione:protein-disulfide oxidoreductase . (wikipedia.org)
  • This enzyme belongs to the family of oxidoreductases , specifically those acting on a sulfur group of donors with a disulfide as acceptor. (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)
  • Until recently, all crystal structures of the NMDA receptor were made by substituting a cysteine for a lysine to create a disulfide bridge and reduce mobility of the receptor. (labroots.com)
  • Allosteric disulfide bonds regulate protein function when they break and/or form. (biomedcentral.com)
  • Functional analysis of the alpha-defensin disulfide array in mouse cryptdin-4. (nih.gov)
  • It is an open question which form of the disulfide is the functional configuration. (biomedcentral.com)
  • A minor population of disulfide bonds serve a functional role. (biomedcentral.com)
  • All disulfides in NMR and X-ray protein structures as well as in refined structure datasets were compared and contrasted for configuration and strain energy. (biomedcentral.com)
  • Moreover, the energies of all twenty types of disulfide bond was higher in NMR structures than X-ray structures, where there was an exponential decrease in the mean strain energy as the incidence of the disulfide type increased. (biomedcentral.com)
  • Evaluation of protein structures for which there are X-ray and NMR models shows that the same disulfide bond can exist in different configurations in different models. (biomedcentral.com)
  • A disulfide bond configuration that is rare in X-ray structures is the -LHStaple. (biomedcentral.com)
  • In NMR structures, this disulfide is characterised by a particularly high potential energy and very short α-carbon distance. (biomedcentral.com)