disulfide bond

(redirected from Disulphide bond)
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disulfide bond

[dī¦səl‚fīd ′bänd]
(organic chemistry)
References in periodicals archive ?
We will probe the electron-transfer and proton-transfer pathway through the enzyme by making single site amino-acid exchanges near the Cys residues and measuring the change in the energetics (electrical voltage) and rate (electrical current) of disulphide bond formation.
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.
In the case of RA, the Pitzalis' group, using in vivo phage display selection in severe combined immunodeficient (SCID) mice transplanted with human synovium, has identified a distinct target for such disease tissue recognised by a cyclic epta-peptide KSTHDRL, known as peptide 3.1 (Lee et al., 2002) constrained by two terminal cysteines that form a disulphide bond. Previous published work from the same group, has also demonstrated the capability of peptide 3.1 to effectively fuse to and deliver the anti-inflammatory cytokine IL-4, directly to RA synovium transplanted into SCID mice and functionally inhibit inflammation in the grafted tissue (Wythe et al., 2013).
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.