disulfide bond

(redirected from Disulphide bonds)
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disulfide bond

[dī¦səl‚fīd ′bänd]
(organic chemistry)
References in periodicals archive ?
10 Briefly, reducible disulphide bonds were first reduced to form free functional thiol groups.
Disulphide bonds are reduced to thiol groups via antioxidant mechanisms, and thiol/disulphide homeostasis is maintained in this way (11).
Sulphydryl and Disulphide Bonds. Sulphydryl and disulphide bond plays an important role in the formation of relatively rigid structures and significantly influences the functional properties of proteins [27].
Formation of gluten network during mixing is enabled through inter- and intramolecular cross linking within monomeric gliadin fractions and within and between glutenin polymers, formed as a consequence of interchange reactions between sulphydryl groups (SH) and disulphide bonds (SS) [1, 2].
Rousseau, "Are disulphide bonds formed during acid gelation of preheated milk?" International Journal of Food Science & Technology, vol.
A possible chemical process behind this is that sulphhydryl groups of Cys633 and Cys856 are initially oxidized by hyperoxia into glutathione-sensitive sulphenic acid, with the subsequent conversion into relatively stable, glutathione-insensitive disulphide bonds. (103) It is still unclear whether these disulphide bonds are formed intermolecularly or intramolecularly by TRPA1 proteins.
[11] The plasma thiol pool is mainly formed by albumin and protein thiols and slightly formed by low molecular weight thiols.12 Thiols can undergo oxidation reaction via oxidants and form disulphide bonds. The formed disulphide bonds can again be reduced to thiol groups; thus, dynamic thiol/disulphide homeostasis is maintained.
Various types of bonds are used in these links: hydrogen bonds between R groups, disulphide bonds between two cysteines molecules, as in the primary structure, ionic bonds between R groups containing amine and carboxyl groups, and hydrophobic reactions between R groups which are non-polar all contribute to holding the tertiary structure of a protein.
This result indicated that this enzyme could not completely cleave the disulphide bonds. Pretreatment of these substrates such as chicken feather, nail and human hair by physical method or reducing agents, or detergents, or activation of the enzyme by adding metal salts are required for the improvement of their degradation (Suntornsuk et al, 2005).
The [alpha]-keratin dimer is stabilized by hydrogen bonds as well as inter- and intramolecular disulphide bonds which are responsible for a compact three-dimensional stable structure [9,10].
Disulphide bonds can prevent partially the unfolding process and form links between protein molecules.