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disulphide
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disulphide
disulphide Chem. (daɪˈsʌlfaɪd) [f. di-2 + sulphide.] A compound in which two atoms of sulphur are united with another element or a radical, as carbon disulphide, CS2. † Formerly, a compound having one atom of sulphur united to two of another element, as disulphide of copper = cuprous sulphide, Cu2S....
Oxford English Dictionary
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Tetraiodoethylene
Another synthesis involves mixing separate solutions of diiodoacetylene and iodine in carbon disulphide. Tetraiodoethylene would be left as a residue after carbon disulphide was evaporated.
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What are the functions of disulphide bonds? What are the functions of disulphide bonds between amino acids in proteins or peptides?
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Disulphide bonds (or bridges) can also hold different subunits of larger protein complexes together, one example for this
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Fibroin
The heavy and light chains are linked by a disulphide bond, and P25 associates with disulphide-linked heavy and light chains by noncovalent interactions
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Sclerotin
In some of the Apterygota, however, at least some of the cross-linking is by disulphide bonds reminiscent of protein cross-linking in the formation of Invertebrate connective tissue proteins based on disulphide links appear to be radically different.
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Where do the electrons and protons formed from biological reactions go? In a reaction like disulphide bond formation protons and electrons are released. These particles are presumably damaging in high levels. What sys...
It shows the oxidation of a pair of thiols to create a disulphide. What is missing from this scheme is the accompanying oxidising agent.
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Pyridine nucleotide-disulphide oxidoreductase domain 1
Pyridine nucleotide-disulphide oxidoreductase domain 1 is a protein that in humans is encoded by the PYROXD1 gene. Function
This gene encodes a nuclear-cytoplasmic pyridine nucleotide-disulphide reductase (PNDR).
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Procedure of diagonal electrophoresis I am learning protein sequencing and it seems that diagonal electrophoresis is a common method in the identification of disulphide bonds (S-S) exist between polypeptides in a prot...
You probably don’t _need_ to oxidize the disulfide bonds rather than reduce them. Performic acid has some potential advantages: * The oxidation products can’t spontaneously reform a disulfide bond whereas the reduction products from a thiolate reductant can. * Oxidation by performic acid causes a si...
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Dc1a
Etymology and chemical structure
Dc1a contains two β-sheets and one β-hairpin loop whereas the sheets are held together by four disulphide bonds. Three of these four disulphide bonds form a classical cysteine knot region (ICK).
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Why is protein cyclisation desirable? There are a number of methods to "cyclize" an existing peptide: * Disulphide bond as described in Disulfide Bond Mimetics: Strategies and Challenges by Gori et al. * "Linchpi...
As described in the abstract of Synthetic Cross-linking of Peptides: Molecular Linchpins for Peptide Cyclization by Derda et al., protein cyclization improves: > resistance to proteolytic degradation and conformational stability. The latter property leads to an increase in binding potency and increa...
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Hsp33
Oxidizing conditions like H2O2 cause disulphide bonds to form in Hsp33, a process that leads to the activation of its chaperone function.
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Carbon Disulphide-MSDS | PDF | Toxicity | Firefighting - Scribd
Product name : Carbon Disulphide. CAS-No. : 75-15-. 1.2 Relevant identified uses of the substance or mixture and uses advised against. Identified uses : Laboratory chemicals, Industrial & for professional use only. 1.3 Details of the supplier of the safety data sheet. Company : Central Drug House (P) Ltd. 7/28 Vardaan House.
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AGR3
AGR3 (Anterior gradient 3, protein disulphide isomerase family member) هوَ بروتين يُشَفر بواسطة جين AGR3 في الإنسان.
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Antifungal protein family
members sharing a structure consisting of five antiparallel beta strands which are highly twisted creating a beta barrel stabilised by four internal disulphide
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Cysteine-rich protein
Cysteine-rich proteins (also cysteine-rich peptide, CRP, disulphide-rich peptide) are small proteins that contain a large number of cysteines. Structure
Disulphides
In an oxidising environment cysteines cross-link to form disulphide bonds.
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