Question

(a) Glutenin, a wheat protein rich in disulfide bonds, is responsible for the cohesive and elastic character of dough made from wheat flour. Similarly, the hard, tough nature of tortoise shell is due to the extensive disulfide bonding in its -keratin. What is the molecular basis for the correlation between disulfide-bond content and mechanical properties of the protein?

Answer 1

Answer: Through extensive bonding

Step-by-step explanation:

Oxidation of two cysteine gives disulphide bonds. They are covalent in nature. Given as;

R-CH2-SH + R'-CH2 +02 = R-CH2-S-S-CH2-R' + H202

They are the stabilizing force behind protein folding the endoplasmic reticulum. Proteins being the backbone of our genetic constitution require disulphide bonding to stabilize the peptide molecules and the extent and number of this bonding determines the Resistance of the protein molecule to extreme conditions e.g extreme heat which denatures proteins and elasticity as well.