disulfide bond

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disulfide bond

[dī¦səl‚fīd ′bänd]

(organic chemistry)

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].

Conformational and Functional Properties of Soybean Proteins Produced by Extrusion-Hydrolysis Approach

(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.

TRP channels in oxygen physiology: distinctive functional properties and roles of TRPA1 in [O.sub.2] sensing

In a disulphide bond disruptive buffer (PP+TH+D) the solubility increases around 16%.

Impact of Hydrolyzed Whey Protein on the Molecular Interactions and Cross-Linking Density in Whey Protein Isolate-Based Films

The cross-linking of polymeric chain due to disulphide bond formation may be responsible for the improved mechanical strength.

Bilayered films based on novel polymer derivative for improved ocular therapy of gatifloxacin

Structural analysis of the CD2 T lymphocyte antigen by site-directed mutagenesis to introduce a disulphide bond into domain 1.

Factors affecting the expression of recombinant glycoproteins

10 Briefly, reducible disulphide bonds were first reduced to form free functional thiol groups.

Thiol disulphide homeostasis in patients with acute myocardial infarction (AMI)

Reactive oxygen species (ROS) forming in an organism cause oxidation and form disulphide bonds by transferring excess electrons to thiols.

A Marker for Evaluation of Oxidative Stress in Patients with Alopecia Areta: Thiol-Disulphide Homeostasis/Alopesi Areata Tanili Hastalarda Oksidatif Stresin Degerlendirilmesinde Bir Belirtec: Tiyol-Disulfid Homeostazi

Disulphide bonds are reduced to thiol groups via antioxidant mechanisms, and thiol/disulphide homeostasis is maintained in this way (11).

The Role of Follicular Fluid Thiol/Disulphide Homeostasis in Polycystic Ovary Syndrome

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].

Biochemical Quality Indicators and Enzymatic Activity of Wheat Flour from the Aspect of Climatic Conditions

Rousseau, "Are disulphide bonds formed during acid gelation of preheated milk?" International Journal of Food Science & Technology, vol.

Fractal Dimension Analysis of Texture Formation of Whey Protein-Based Foods

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