disulfide bond

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disulfide bond

[dī¦səl‚fīd ′bänd]
(organic chemistry)
McGraw-Hill Dictionary of Scientific & Technical Terms, 6E, Copyright © 2003 by The McGraw-Hill Companies, Inc.
References in periodicals archive ?
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].
(48) In addition, the activation of chicken TRPV1 was proposed to be a consequence of dimerization through the formation of a disulphide bond. (49) Because all of the above models of oxidation-induced TRPV1 activation are based on Cys mutagenesis, it is still possible that the suppression of activation is due to non-specific structural disruption of the protein.
In a disulphide bond disruptive buffer (PP+TH+D) the solubility increases around 16%.
The cross-linking of polymeric chain due to disulphide bond formation may be responsible for the improved mechanical strength.
Structural analysis of the CD2 T lymphocyte antigen by site-directed mutagenesis to introduce a disulphide bond into domain 1.
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).
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.