Nucleic Acid Renaturation
Starch
Amylases
Glucan 1,4-alpha-Glucosidase
Half-Life
Anemone
alpha-Amylases
Molecular Sequence Data
ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation. A novel multi-chaperone system from Escherichia coli. (1/215)
ClpB is a heat-shock protein from Escherichia coli with an unknown function. We studied a possible molecular chaperone activity of ClpB in vitro. Firefly luciferase was denatured in urea and then diluted into the refolding buffer (in the presence of 5 mM ATP and 0.1 mg/ml bovine serum albumin). Spontaneous reactivation of luciferase was very weak (less than 0.02% of the native activity) because of extensive aggregation. Conventional chaperone systems (GroEL/GroES and DnaK/DnaJ/GrpE) or ClpB alone did not reactivate luciferase under those conditions. However, ClpB together with DnaK/DnaJ/GrpE greatly enhanced the luciferase activity regain (up to 57% of native activity) by suppressing luciferase aggregation. This coordinated function of ClpB and DnaK/DnaJ/GrpE required ATP hydrolysis, although the ClpB ATPase was not activated by native or denatured luciferase. When the chaperones were added to the luciferase refolding solutions after 5-25 min of refolding, ClpB and DnaK/DnaJ/GrpE recovered the luciferase activity from preformed aggregates. Thus, we have identified a novel multi-chaperone system from E. coli, which is analogous to the Hsp104/Ssa1/Ydj1 system from yeast. ClpB is the only known bacterial Hsp100 protein capable of cooperating with other heat-shock proteins in suppressing and reversing protein aggregation. (+info)Activation of p90RSK and cAMP response element binding protein in stimulated neutrophils: novel effects of the pyridinyl imidazole SB 203580 on activation of the extracellular signal-regulated kinase cascade. (2/215)
Neutrophils stimulated with the chemoattractant FMLP or the phorbol ester PMA are known to exhibit activation of a 90-kDa renaturable protein kinase. Activation of this kinase was maximal at approximately 1-3 min after cell stimulation and the time course for activation was similar to that of the extracellular-regulated kinases (ERKs) and p38-mitogen activated protein kinase (p38MAPK). Compounds that block activation of ERK-1/2 (PD 98059) or that inhibit the activity of p38MAPK (SB 203580) blocked activation of this 90-kDa kinase. SB 203580 is a highly selective inhibitor of p38MAPK in vitro and is under intense study as a lead compound for developing novel anti-inflammatory agents. However, we demonstrate that SB 203580 at concentrations >/=10 microM can also inhibit activation of ERK-1/2 in neutrophils. An Ab to the protein kinase p90RSK2 (also referred to as MAPKAP-K1b, or p90rsk) immunoprecipitated the active 90-kDa kinase from lysates of stimulated neutrophils. No activity was observed for this enzyme in immunoprecipitates obtained from unstimulated cells, and the amounts of activity were markedly reduced if the cells were treated with PD 98059 or SB 203580 before stimulation. Neutrophils stimulated with FMLP exhibited phosphorylation of the cAMP response element binding protein (CREB), and this reaction was inhibited by SB 203580 and PD 98059. These data establish that the renaturable 90-kDa protein kinase is p90RSK2 and that CREB may be a substrate for this enzyme in these cells. Novel effects of compound SB 203580 on stimulated neutrophils are also described. (+info)Renaturation of recombinant Treponema pallidum rare outer membrane protein 1 into a trimeric, hydrophobic, and porin-active conformation. (3/215)
We have previously observed that while native Treponema pallidum rare outer membrane protein 1 (Tromp1) is hydrophobic and has porin activity, recombinant forms of Tromp1 do not possess these properties. In this study we show that these properties are determined by conformation and can be replicated by proper renaturation of recombinant Tromp1. Native Tromp1, but not the 47-kDa lipoprotein, extracted from whole organisms by using Triton X-114, was found to lose hydrophobicity after treatment in 8 M urea, indicating that Tromp1's hydrophobicity is conformation dependent. Native Tromp1 was purified from 0.1% Triton X-100 extracts of whole organisms by fast-performance liquid chromatography (FPLC) and shown to have porin activity in planar lipid bilayers. Cross-linking studies of purified native Tromp1 with an 11 A cross-linking agent showed oligomeric forms consistent with dimers and trimers. For renaturation studies of recombinant Tromp1 (rTromp1), a 31,109-Da signal-less construct was expressed in Escherichia coli and purified by FPLC. FPLC-purified rTromp1 was denatured in 8 M urea and then renatured in the presence of 0.5% Zwittergent 3,14 during dialysis to remove the urea. Renatured rTromp1 was passed through a Sephacryl S-300 gel exclusion column previously calibrated with known molecular weight standards. While all nonrenatured rTromp1 eluted from the column at approximately the position of the carbonic anhydrase protein standard (29 kDa), all renatured rTromp1 eluted at the position of the phosphorylase b protein standard (97 kDa), suggesting a trimeric conformation. Trimerization was confirmed by using an 11 A cross-linking agent which showed both dimers and trimers similar to that of native Tromp1. Triton X-114 phase separations showed that all of renatured rTromp1, but none of nonrenatured rTromp1, phase separated exclusively into the hydrophobic detergent phase, similar to native Tromp1. Circular dichroism of nonrenatured and renatured rTromp1 showed a marked loss in alpha-helical secondary structure of renatured rTromp1 compared to the nonrenatured form. Finally, renatured rTromp1, but not the nonrenatured form, showed porin activity in planar liquid bilayers. These results demonstrate that proper folding of rTromp1 results in a trimeric, hydrophobic, and porin-active conformation similar to that of the native protein. (+info)Effects of macromolecular crowding on protein folding and aggregation. (4/215)
We have studied the effects of polysaccharide and protein crowding agents on the refolding of oxidized and reduced hen lysozyme in order to test the prediction that association constants of interacting macromolecules in living cells are greatly increased by macromolecular crowding relative to their values in dilute solutions. We demonstrate that whereas refolding of oxidized lysozyme is hardly affected by crowding, correct refolding of the reduced protein is essentially abolished due to aggregation at high concentrations of crowding agents. The results show that the protein folding catalyst protein disulfide isomerase is particularly effective in preventing lysozyme aggregation under crowded conditions, suggesting that crowding enhances its chaperone activity. Our findings suggest that the effects of macromolecular crowding could have major implications for our understanding of how protein folding occurs inside cells. (+info)Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB. (5/215)
We systematically analyzed the capability of the major cytosolic chaperones of Escherichia coli to cope with protein misfolding and aggregation during heat stress in vivo and in cell extracts. Under physiological heat stress conditions, only the DnaK system efficiently prevented the aggregation of thermolabile proteins, a surprisingly high number of 150-200 species, corresponding to 15-25% of detected proteins. Identification of thermolabile DnaK substrates by mass spectrometry revealed that they comprise 80% of the large (>/=90 kDa) but only 18% of the small (+info)Stress-associated endoplasmic reticulum protein 1 (SERP1)/Ribosome-associated membrane protein 4 (RAMP4) stabilizes membrane proteins during stress and facilitates subsequent glycosylation. (6/215)
Application of differential display to cultured rat astrocytes subjected to hypoxia allowed cloning of a novel cDNA, termed stress-associated endoplasmic reticulum protein 1 (SERP1). Expression of SERP1 was enhanced in vitro by hypoxia and/or reoxygenation or other forms of stress, causing accumulation of unfolded proteins in endoplasmic reticulum (ER) stress, and in vivo by middle cerebral artery occlusion in rats. The SERP1 cDNA encodes a 66-amino acid polypeptide which was found to be identical to ribosome-associated membrane protein 4 (RAMP4) and bearing 29% identity to yeast suppressor of SecY 6 protein (YSY6p), suggesting participation in pathways controlling membrane protein biogenesis at ER. In cultured 293 cells subjected to ER stress, overexpression of SERP1/RAMP4 suppressed aggregation and/or degradation of newly synthesized integral membrane proteins, and subsequently, facilitated their glycosylation when the stress was removed. SERP1/RAMP4 interacted with Sec61alpha and Sec61beta, which are subunits of translocon, and a molecular chaperon calnexin. Furthermore, Sec61alpha and Sec61beta, but not SERP1/RAMP4, were found to associate with newly synthesized integral membrane proteins under stress. These results suggest that stabilization of membrane proteins in response to stress involves the concerted action of a rescue unit in the ER membrane comprised of SERP1/RAMP4, other components of translocon, and molecular chaperons in ER. (+info)Chaperone properties of bacterial elongation factor EF-G and initiation factor IF2. (7/215)
Elongation factor G(EF-G) and initiation factor 2 (IF2) are involved in the translocation of ribosomes on mRNA and in the binding of initiator tRNA to the 30 S ribosomal subunit, respectively. Here we report that the Escherichia coli EF-G and IF2 interact with unfolded and denatured proteins, as do molecular chaperones that are involved in protein folding and protein renaturation after stress. EF-G and IF2 promote the functional folding of citrate synthase and alpha-glucosidase after urea denaturation. They prevent the aggregation of citrate synthase under heat shock conditions, and they form stable complexes with unfolded proteins such as reduced carboxymethyl alpha-lactalbumin. Furthermore, the EF-G and IF2-dependent renaturations of citrate synthase are stimulated by GTP, and the GTPase activity of EF-G and IF2 is stimulated by the permanently unfolded protein, reduced carboxymethyl alpha-lactalbumin. The concentrations at which these chaperone-like functions occur are lower than the cellular concentrations of EF-G and IF2. These results suggest that EF-G and IF2, in addition to their role in translation, might be implicated in protein folding and protection from stress. (+info)cis and trans factors affecting Mos1 mariner evolution and transposition in vitro, and its potential for functional genomics. (8/215)
Mos1 and other mariner / Tc1 transposons move horizon-tally during evolution, and when transplanted into heterologous species can transpose in organisms ranging from prokaryotes to protozoans and vertebrates. To further develop the Drosophila Mos1 mariner system as a genetic tool and to probe mechanisms affecting the regulation of transposition activity, we developed an in vitro system for Mos1 transposition using purified transposase and selectable Mos1 derivatives. Transposition frequencies of nearly 10(-3)/target DNA molecule were obtained, and insertions occurred at TA dinucleotides with little other sequence specificity. Mos1 elements containing only the 28 bp terminal inverted repeats were inactive in vitro, while elements containing a few additional internal bases were fully active, establishing the minimal cis -acting requirements for transposition. With increasing transposase the transposition frequency increased to a plateau value, in contrast to the predictions of the protein over-expression inhibition model and to that found recently with a reconstructed Himar1 transposase. This difference between the 'natural' Mos1 and 'reconstructed' Himar1 transposases suggests an evolutionary path for down-regulation of mariner transposition following its introduction into a naive population. The establishment of the cis and trans requirements for optimal mariner transposition in vitro provides key data for the creation of vectors for in vitro mutagenesis, and will facilitate the development of in vivo systems for mariner transposition. (+info)Protein renaturation is the process of restoring the native, functional structure of a protein that has been denatured due to exposure to external stressors such as changes in temperature, pH, or the addition of chemical agents. Denaturation causes proteins to lose their unique three-dimensional structure, which is essential for their proper function. Renaturation involves slowly removing these stressors and allowing the protein to refold into its original configuration, restoring its biological activity. This process can be facilitated by various techniques, including dialysis, dilution, or the addition of specific chemical chaperones.
Nucleic acid renaturation, also known as nucleic acid reassociation or hybridization, is the process of rejoining two complementary single-stranded nucleic acids (DNA or RNA) to form a double-stranded structure. This process occurs naturally in cells during transcription and DNA replication, but it can also be performed in vitro as a laboratory technique.
Renaturation typically involves denaturing the double-stranded nucleic acids into single strands by heat or chemical methods, followed by controlled cooling or modification of conditions to allow the complementary strands to find each other and reanneal. The rate and specificity of renaturation can be used to study the relatedness and concentration of nucleic acid sequences in a sample.
In molecular biology research, nucleic acid renaturation is often used in techniques such as Southern blotting, Northern blotting, and polymerase chain reaction (PCR) to detect and analyze specific DNA or RNA sequences.
I'm happy to help! However, it seems there might be a bit of confusion here. Starch is not typically considered a medical term, but rather a nutritional and biochemical concept. Here's a brief explanation:
Starch is a complex carbohydrate that serves as the primary form of energy storage in plants. It is made up of long chains of glucose molecules and can be found in various foods such as grains, legumes, fruits, and vegetables. Amylase, an enzyme present in our saliva and digestive system, helps break down starch into simpler sugars during the digestion process so that our bodies can absorb them for energy.
I hope this clarifies any confusion! If you have any other questions or need further information on a medical topic, please don't hesitate to ask.
Amylases are enzymes that break down complex carbohydrates, such as starch and glycogen, into simpler sugars like maltose, glucose, and maltotriose. There are several types of amylases found in various organisms, including humans.
In humans, amylases are produced by the pancreas and salivary glands. Pancreatic amylase is released into the small intestine where it helps to digest dietary carbohydrates. Salivary amylase, also known as alpha-amylase, is secreted into the mouth and begins breaking down starches in food during chewing.
Deficiency or absence of amylases can lead to difficulties in digesting carbohydrates and may cause symptoms such as bloating, diarrhea, and abdominal pain. Elevated levels of amylase in the blood may indicate conditions such as pancreatitis, pancreatic cancer, or other disorders affecting the pancreas.
Glucan 1,4-alpha-glucosidase, also known as amyloglucosidase or glucoamylase, is an enzyme that catalyzes the hydrolysis of 1,4-glycosidic bonds in starch and other oligo- and polysaccharides, breaking them down into individual glucose molecules. This enzyme specifically acts on the alpha (1->4) linkages found in amylose and amylopectin, two major components of starch. It is widely used in various industrial applications, including the production of high fructose corn syrup, alcoholic beverages, and as a digestive aid in some medical supplements.
In the context of pharmacology, "half-life" refers to the time it takes for the concentration or amount of a drug in the body to be reduced by half during its elimination phase. This is typically influenced by factors such as metabolism and excretion rates of the drug. It's a key factor in determining dosage intervals and therapeutic effectiveness of medications, as well as potential side effects or toxicity risks.
I am not aware of a medical definition for the term "Anemone." The term "anemone" is typically used to refer to a type of marine or terrestrial flowering plant, also known as windflower. It is not a term that is commonly used in medical contexts. If you have any specific concerns about a medical condition or issue, I would be happy to try and help you with that instead.
Alpha-amylases are a type of enzyme that breaks down complex carbohydrates, such as starch and glycogen, into simpler sugars like maltose, maltotriose, and glucose. These enzymes catalyze the hydrolysis of alpha-1,4 glycosidic bonds in these complex carbohydrates, making them more easily digestible.
Alpha-amylases are produced by various organisms, including humans, animals, plants, and microorganisms such as bacteria and fungi. In humans, alpha-amylases are primarily produced by the salivary glands and pancreas, and they play an essential role in the digestion of dietary carbohydrates.
Deficiency or malfunction of alpha-amylases can lead to various medical conditions, such as diabetes, kidney disease, and genetic disorders like congenital sucrase-isomaltase deficiency. On the other hand, excessive production of alpha-amylases can contribute to dental caries and other oral health issues.
Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.
Doughnut
EF-Tu
Sulfolobus solfataricus
Southwestern blot
Nucleic acid quantitation
HSPBP1
TPM2
Ribonuclease T1
MAP2K1
Renaturation
Denaturation (biochemistry)
Nucleic acid thermodynamics
Piet Borst
Heterologous expression
Cruciform DNA
Inclusion bodies
Cyanase
Prion
Q-FISH
TPM1
Restriction map
Neurotrophin-3
Condensin
Mutation
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Denaturation10
- and the vessel walls are fused through compression, protein denaturation, and then renaturation. (medscape.com)
- Denaturation can occur when proteins are exposed to certain elements such as high or low temperatures, extreme pH levels, sunlight radiation, or mechanical agitation. (gogood.co.nz)
- The enzymes in your digestive system that handle proteins rely on your gut health and the extent of protein denaturation. (gogood.co.nz)
- Denaturation of whey protein isn't exclusive to the manufacturing process but can happen at any time. (gogood.co.nz)
- When we refer to protein denaturation, we mean the process of proteins breaking down and reorganizing their structure. (gogood.co.nz)
- It is a natural occurrence for proteins, but the extent of denaturation and its impact on bioavailability vary. (gogood.co.nz)
- However, the scientific community has not reached a definitive conclusion on the impact of protein denaturation on bioavailability. (gogood.co.nz)
- DNA denaturation and renaturation processes are used for genetic research and studies. (vedantu.com)
- Denaturation and renaturation kinetics are used to determine the size and complexity of the genome. (vedantu.com)
- It was therefore extracted after a step of denaturation/renaturation. (her2-receptor.com)
Kinetics1
- a method to distinguish between highly repetitive and low copy DNA sequences, which uses the principle of DNA renaturation kinetics, in which the rate at which a particular single-stranded sequence returns to the double-stranded state depends on the number of times it is found in the genome. (integratedbreeding.net)
Soluble5
- The efficient refolding of proteins from inclusion bodies is becoming an important tool that can provide soluble native proteins for structural and functional studies. (nih.gov)
- If the protein expresses as inclusion bodies, refolding will be attempted to make the protein soluble. (biozoomer.com)
- The enzyme is a relatively hydrophobic homodimeric intracellular protein difficult to express in the soluble functionally active form. (biomedcentral.com)
- The Rapid GST Inclusion Body Solubilization and Renaturation Kit is designed to retrieve expressed GST fusion proteins in soluble form after lysis and extraction procedures. (bio-connect.nl)
- All except LIR-4 (which appears to encode a soluble molecule) encode type-1 transmembrane proteins, containing either two or four immunoglobulin superfamily (IgSF) domains in their extracellular regions. (biomedcentral.com)
Recombinant proteins3
- From 2007 to 2017, we have successfully developed more than 4000 recombinant proteins expressed in E. coli, which contain hundreds of active proteins with high purity. (cusabio.com)
- Recombinant proteins expressed in bacteria often form inclusion bodies, especially when they are expressed at high levels. (bio-connect.nl)
- The portrayed recombinant proteins was purified using Ni-NTA beads (Qiagen) under denaturing circumstances, and renatured by sequential dilution and focus in renaturation buffer (PBS, pH 7.0, containing 2 mM MgCl2, 0.5 mM PMSF, 0.005% Tween 20, 10 mM DTT, protease inhibitor cocktail). (conferencedequebec.org)
Substrate5
- This doesn't alter the protein, it simply makes it less likely for the substrate to bind to its enzyme. (fiveable.me)
- Further investigations of the substrate specificity revealed for the first time the muscle proteins actin and myosin as being substrates of fibronectinase. (uni-bielefeld.de)
- The apical domain is located at the entrance of the cylinder and binds GroES and substrate proteins using hydrophobic surfaces [6,7]. (scirp.org)
- During the folding cycle of substrate proteins by GroEL, GroES and ATP bind to one of the two rings of the GroEL molecule, called the cis-ring, and form a bullet-type complex [9-13]. (scirp.org)
- Codding JA, Israel BA, Thorpe C. Protein substrate discrimination in the quiescin sulfhydryl oxidase (QSOX) family. (jefferson.edu)
Conformation2
- Extracted proteins on the membrane are renatured to allow them to regain their native conformation. (labtestsguide.com)
- Most protein is folded in defined structures which are maintained by a large number of relatively weak non-covalent bond and the biological activities of the protein depend on the correctly folded conformation. (ukessays.com)
Purification8
- Our method is a combination of an 'artificial chaperone-assisted refolding' method previously proposed and affinity chromatography to take advantage of a chromatographic step: less time-consuming, no filtration or concentration, with the additional benefit of protein purification. (nih.gov)
- Refolding and simultaneous purification of recombinant human proinsulin from inclusion bodies on protein-folding liquid-chromatography columns. (nih.gov)
- CUSABIO has extensive experience and be very professional in E. coli protein expression and purification. (cusabio.com)
- We can solve various difficult problems during the protein expression and purification process. (cusabio.com)
- Characteristics: The protein is a fusion protein, and digested with PreScission protease overnight through the GST affinity chromatography column, subsequently with one-step purification to obtain protein without tag. (cusabio.com)
- Our Guaranteed Recombinant Protein Expression Service Package consists of codon optimization service, followed by gene synthesis and subcloning, all the way through protein expression and purification. (biozoomer.com)
- 1993. Purification and properties of a cruciform DNA binding protein from Ustilago maydis. . (cornell.edu)
- After 6 h, His6-SarA and His6-Stk1 were extracted and purified using an immobilized Zn2+ matrix (Qiagen), suitable for the purification of fusion proteins carrying a poly-histidine tag. (her2-receptor.com)
Amino acid2
- A protein chain folds into a distinct three dimensional shape that is stabilized by non-covalent interactions between the regions of linear sequences of amino acid and is specified by amino acid sequences. (ukessays.com)
- It indicates the covalent structures of the protein, sequences of amino acid residues and position of the any interchange links such as disulfide bond. (ukessays.com)
Dilution1
- Refolding protein with purity greater than 90% is obtained by dilution renaturation, dialysis renaturation, column chromatography renaturation and so on. (cusabio.com)
Actin1
- The following genes were expressed at lower levels in the flow diverter group compared with the coiled aneurysm group: proteinases (matrix metalloproteinases 2 and 9), cellular markers (endothelial nitric oxide synthase and smooth muscle actin), and structural proteins (collagens and fibronectin). (bmj.com)
Bacteria1
- The system is mainly used for antigen preparation, ligand preparation, and expression of cytokines and bacteria (Staphylococcus aureus, Escherichia coli, etc.) proteins. (cusabio.com)
Processes3
- Northwestern blotting is used to identify and characterize RNA-protein interactions, helping researchers understand the roles of specific RNA molecules in various biological processes. (labtestsguide.com)
- Northwestern blotting is applied in various fields, including molecular biology, genetics, and biochemistry, to investigate RNA-protein interactions in processes such as transcriptional regulation, RNA processing, and RNA localization. (labtestsguide.com)
- Processes involved in the formation of TERTIARY PROTEIN STRUCTURE. (jefferson.edu)
Structural2
- One major bottleneck in protein production in Escherichia coli for structural genomics projects is the formation of insoluble protein aggregates (inclusion bodies). (nih.gov)
- All proteins of this family share a structural motif called \immunoglobulin domain » [9], which structure will be analysed more in detail in Chapter 4 and Chapter 5. (bestpfe.com)
Occur2
- If RNA-protein interactions occur, the RNA probe will bind to the target protein. (labtestsguide.com)
- 2. When Does Renaturation Occur? (vedantu.com)
Sequences5
- The renaturation rate is directly proportional to the number of complementary sequences present. (vedantu.com)
- The three dimensional structures of proteins reflects the underlying structures basically on the variations on the sequences and the length of amino acids. (ukessays.com)
- Protein consists of long polypeptide chains to determine the sequences of the amino acids. (ukessays.com)
- The sequences of amino acids in a polypeptide chain determine the final three dimensional structure of the protein which ultimately functions for various biological activities in the living organisms. (ukessays.com)
- 1986. Homologous pairing of DNA molecules by Ustilago rec1 protein is promoted by sequences of Z-DNA. . (cornell.edu)
Genes3
- 29. Expression and distribution of three heat shock protein genes under heat shock stress and under exposure to Vibrio harveyi in Penaeus monodon. (nih.gov)
- 33. Molecular Cloning and mRNA Expression of Heat Shock Protein Genes and Their Response to Cadmium Stress in the Grasshopper Oxya chinensis. (nih.gov)
- Genes related to inflammation (tumor necrosis factor α and monocyte chemoattractant protein 1) were upregulated in flow diverter treated aneurysms compared with coil embolized aneurysms. (bmj.com)
Molecule4
- A labeled RNA molecule is used as a probe to detect RNA-protein interactions. (labtestsguide.com)
- Northwestern blotting can help identify the specific regions of an RNA molecule that interact with a protein. (labtestsguide.com)
- They determined that no detectable differences could be found between the two protein preparations, and concluded that the operator locus, the region of DNA at one end of an operon that acts as the binding site for repressor proteins, did not specify any part of the structure of the beta-galactosidase molecule. (nih.gov)
- It is a sequence which determines the further level of organization of the protein molecule. (ukessays.com)
Proteolytic1
- In the context of induced cathepsin D release, e. g. from granulocytes under inflammatory conditions, these results indicate an increase in specific proteolytic potential against muscular proteins in dystrophic diseases by the release of cryptic fibronectinase. (uni-bielefeld.de)
HSP604
- HSP60 was found in the mammalian mitochondrial matrix as a Pl protein precursor [14-16]. (scirp.org)
- HSP60 plays an essential role in assisting with the folding of the newly synthesized polypeptides and refolding of the denatured proteins in the cells [14-17]. (scirp.org)
- Previously, we found that a major protein was directly bound to mizoribine, and this protein was identified as HSP60 [25]. (scirp.org)
- Additionally, we have shown that mizoribine inhibits the suppression of protein aggregation by HSP60 [25]. (scirp.org)
Polypeptides1
- Thus, macromolecular compounds do not diffuse as easily through the matrix in which they are contained and they tend to be susceptible to deactivation during preparation of the delivery device and during release from the device, e.g. polypeptides and proteins are denatured. (justia.com)
Suitable2
- Note: This risk-free custom protein service is only suitable for proteins within 800aa. (cusabio.com)
- Renaturation occurs when the denatured DNAs are cooled in suitable conditions. (vedantu.com)
Inclusion bodies1
- The recombinant pFN protein fragment was isolated from inclusion bodies, subjected to folding and autocatalytic degradation in the presence of Ca2+, and yielded an active enzyme capable of digesting fibronectin. (uni-bielefeld.de)
Quaternary1
- The structures include primary, secondary, tertiary and the quaternary structures of the proteins. (ukessays.com)
Biochemical1
- Mechanotransduction involving multimodular proteins: converting force into biochemical signals. (uni-bielefeld.de)
Tissues3
- 25. [Comparative study of expression levels of the major human heat shock proteins in cancer and normal tissues]. (nih.gov)
- Proteins are extracted from biological samples (e.g., cells or tissues) of interest. (labtestsguide.com)
- Prior studies to this article by Anfinsen, Epstein, and Goldberger established that the time required for synthesizing a chain of protein such as ribonuclease in the tissues of higher organisms would be approximately two minutes. (nih.gov)
Structures4
- When the second, third, or fourth protein structures are permanently deformed, your body may struggle to recognize the nutritional value of the protein. (gogood.co.nz)
- The amino acids sequence is a form that diverts the folding of the protein into its unique three dimensional structures and ultimately determines the function protein. (ukessays.com)
- To represent the primary structures of the protein, the N-terminus is always written on the left sides and the C-terminus is on the right end of the chain. (ukessays.com)
- A single peptide may contain multiple types of secondary structures in various protein of the chain depending on its structures. (ukessays.com)
Target protein2
- The E. coli expression system is regarded as the most commonly used, economical, and classical expression system because of its simple structure, clear genetic background, high yield of target protein, and its short culture period. (cusabio.com)
- These proteins may include the target protein suspected to interact with the RNA. (labtestsguide.com)
Temperature3
- Researchers can assess the stability of RNA-protein complexes by varying experimental conditions, such as salt concentrations or temperature. (labtestsguide.com)
- Renaturation also depends on temperature, pH, length and constituents of the DNA structure. (vedantu.com)
- Manipulation of culture conditions such as addition of sorbitol to induce intracellular accumulation of osmolytes, addition of benzyl alcohol to induce chaperone expression, or lowering incubation temperature to slow down protein expression and folding rates all failed to increase the active D-PhgAT yield. (biomedcentral.com)
Aggregation1
- This rst introductory chapter is focused on the basic mechanisms that are at the origin of protein aggregation. (bestpfe.com)
Enzymes1
- Proteins are fundamental components of all living cells and include many substances, such as enzymes, hormones, and antibodies, that are necessary for the proper functioning of an organism. (wordnik.com)
Coli2
- In recent decades, E. coli expression system has also been developed and improved continuously, and been used intensively by scientific researchers and industrial users for a large number of recombinant protein expression. (cusabio.com)
- With the optimized gene dosage and chaperone combinations, P. pastoris can be attractive for intracellular expression of bacterial proteins since it can grow to a very high cell density which is translated into the higher volumetric product yield than the E. coli or other bacterial systems. (biomedcentral.com)
Structure of the protein2
- It's because hydrogen bonds can be altered by the pH level, thus altering the structure of the protein (and you guessed it) and thus its function. (fiveable.me)
- Inhibitors don't denature the protein, but they do alter the structure of the protein. (fiveable.me)
Vitro4
- This checkpoint has been reconstituted in vitro in Xenopus egg extracts, and here we use antibodies to Xenopus Bub3 (XBub3) to show that this protein is required for both the activation and the maintenance of a spindle checkpoint arrest in egg extracts. (biologists.com)
- Since condensin has ability to remove ssDNA-binding proteins and RNA from unwound ssDNAs or DNA-RNA hybrids in vitro , we propose a model that condensin-mediated removal of mitotic transcripts from chromosomal DNA is the primary mechanism of sister chromatid separation. (biorxiv.org)
- We studied the effect of NM on human colon cancer cell line HCA-7 in vitro by measuring cancer cell proliferation, invasion, and expression of pro-inflammatory COX-2 and COX-1 proteins. (jcmnh.org)
- 3 In the current study, we investigated the antitumor potential of the nutrient mixture (NM) on human colon cancer cell line HCA-7 in vitro by measuring cell proliferation, Matrigel™ invasion, and the effect of NM on markers of inflammation: cyclooxygenase COX-1 and COX-2 protein expression. (jcmnh.org)
Folding8
- The current development of ab initio protein folding tools allows one to predict the structure. (nature.com)
- For tag-free packages, we can provide service start with tag-free protein expression, and purified by SEC and ion exchange to ensure proper native folding, or start with fusion tag expression, and purified by tag removal, HIC, SEC or IEX to ensure proper native folding. (biozoomer.com)
- Because the folding of protein is very complex, different elements of structure are considered separately. (ukessays.com)
- Protein folding and stability: to aggregate or not to aggregate? (bestpfe.com)
- We will particularly justify the need to control protein folding and stability. (bestpfe.com)
- Protein Folding" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus, MeSH (Medical Subject Headings) . (jefferson.edu)
- This graph shows the total number of publications written about "Protein Folding" by people in this website by year, and whether "Protein Folding" was a major or minor topic of these publications. (jefferson.edu)
- Below are the most recent publications written about "Protein Folding" by people in Profiles. (jefferson.edu)
Gene1
- 1994. The REC2 gene encodes the homologous pairing protein of Ustilago maydis. . (cornell.edu)
Purity1
- Protein purity is determined by SDS-PAGE, and quantity is determined by Bradford/BCA/A280 assay. (biozoomer.com)
Encodes1
- the part of a DNA sequence which encodes a protein (usually in conjunction with other exons). (integratedbreeding.net)
Antibodies2
- A particular attention is paid to proteins of therapeutic interest, notably antibodies. (bestpfe.com)
- Antibodies are glycoproteins (i.e. proteins that contain oligosaccharides chains covalently attached to the polypeptide backbone) belonging to the superfamily of \immunoglobu-lins » (Ig). (bestpfe.com)
Heat shock p4
- 31. Heat-shock protein 70-2 (HSP70-2) expression in bladder urothelial carcinoma is associated with tumour progression and promotes migration and invasion. (nih.gov)
- 34. [Expressions of heat shock protein in cervical cancer and precancerosis]. (nih.gov)
- 39. Heat shock protein expression induced by percutaneous radiofrequency ablation of hepatocellular carcinoma in vivo. (nih.gov)
- 40. Heat shock protein expression in human gliomas. (nih.gov)
Oxygen1
- The sequence of amino acids produce a strong, fibrous structure found in hair, wool and some protein that transport oxygen in the blood. (ukessays.com)
Assay5
- Northwestern blotting, also known as the northwestern assay, is a hybrid analytical technique of the western blot and the northern blot, and is used in molecular biology to detect interactions between RNA and proteins. (labtestsguide.com)
- Northwestern blotting is often complemented by other techniques like RNA immunoprecipitation (RIP) and electrophoretic mobility shift assay (EMSA) to further validate and characterize RNA-protein interactions. (labtestsguide.com)
- Protein concentration was determined using the Coomassie Plus Protein Assay (Pierce). (her2-receptor.com)
- Proteins Phosphatase Assays PTEN dephosphorylation of Shc and FAK had been analyzed using an Akap7 in blot phosphatase assay as defined (Tamura et al. (conferencedequebec.org)
- Protein misfolding detected early in pathogenesis of transgenic mouse model of Huntington disease using amyloid seeding assay. (jefferson.edu)
Modulation1
- modulation by chromatin associated proteins. (cornell.edu)
Regulation2
- In dieser Arbeit wurden neue Erkenntnisse zur endogenen Regulation von Sirtuinen durch das Protein AROS und zur Sirtuinmodulation durch Kleinmoleküle gewonnen. (uni-bayreuth.de)
- 1984. Hysteretic regulation of Ustilago rec1 protein during synapsis. . (cornell.edu)
Molecules3
- Northwestern blotting is a laboratory technique used to study RNA-protein interactions by detecting and characterizing the binding of RNA molecules to specific proteins. (labtestsguide.com)
- Northwestern blotting is a crucial tool for investigating how RNA molecules interact with specific proteins in cells. (labtestsguide.com)
- 1983. Topological linkage of circular DNA molecules promoted by Ustilago rec 1 protein and topoisomerase. . (cornell.edu)
Chains1
- These proteins of ca. 150 kDa molecular weight consist of a heterotetramer of two identical light chains (MW ∼ 25 kDa) and two identical heavy chains (MW ∼ 50 kDa) held together by disulfide bridges (Figure 1.1) [11]. (bestpfe.com)
Preparations1
- To refine and independently validate the model, we determined protein-related copper stoichiometries on purified receptor preparations and explored the helix arrangement by tryptophan scanning mutagenesis. (nature.com)
Interactions5
- Northwestern blotting is a specialized technique used to study RNA-protein interactions. (labtestsguide.com)
- Positive and negative controls are used to validate the specificity of RNA-protein interactions. (labtestsguide.com)
- Researchers can compare RNA-protein interactions between different samples or conditions to gain insights into regulatory mechanisms. (labtestsguide.com)
- In some cases, crosslinking agents may be used to stabilize RNA-protein interactions before performing Northwestern blotting. (labtestsguide.com)
- Developed to study RNA-protein interactions, with "Northwestern" as an analogy to "Western" and "Southern" blotting. (labtestsguide.com)
Process4
- After electrophoresis, proteins are transferred from the gel to a membrane, typically using a process similar to Western blotting. (labtestsguide.com)
- Separate single strands rewind on cooling and the process is known as renaturation. (vedantu.com)
- If the DNA isn't completely denatured, the renaturation process is fast and a one-step process, but if the DNAs are completely denatured then the renaturation process occurs in a two-step process. (vedantu.com)
- By the process of renaturation, absorption of UV (260nm) decreases and viscosity increases again. (vedantu.com)
Specific3
- Terms like "damaged protein," "denatured peptides," and "altered whey protein fractions" all refer to the same concept: whey protein and its specific fractions are delicate and prone to deformation. (gogood.co.nz)
- Involvement of mitogen-activated protein kinases (MAPK) signaling pathways was evaluated by Western blot and using specific inhibitors. (biomedcentral.com)
- Towards this end, we have generated an a1(IV)NC1 transgenic mouse model and adenoviruses, cloned and expressed a1(IV)NC1 in the baculovirus expression system and will use this protein for studies outlined in the specific aims. (grantome.com)
Separation1
- Separation is based on charge and size, allowing proteins to retain their RNA-binding activity. (labtestsguide.com)
Studies2
- Only one form of XBub3 is apparent in Xenopus tissue culture (XTC) cells,and localisation studies reveal that, unlike the Mad proteins, which are concentrated at the nuclear periphery, XBub3 is diffusely localised throughout the nucleus during interphase. (biologists.com)
- Subsequent studies would find that such motile proteins as staphylococcal nuclease or myoglobin could undergo virtually complete renaturation in only a few seconds or less. (nih.gov)
Cells1
- 30. Heat shock proteins and survivin: relationship and effects on proliferation index of retinoblastoma cells. (nih.gov)