Some natural proteins are rich in disulfide bonds, and their mechanical properties (tensile strength, viscosity, hardness, etc.) are correlated with the degree of disulfide bonding. (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 oftortoise shell is due to the extensive disulfide bonding in its α-keratin. What is the molecular basis for the correlation between disulfide-bond content and mechanical properties of the protein?(b) Most globular proteins are denatured and lose their activity when briefly heated to 65 °C. However, globular proteins that contain multiple disulfide bonds often must be heated longer at higher temperatures to denature them. One such protein is bovine pancreatic trypsin inhibitor (BPTI), which has 58 amino acid residues in a single chain andcontains three disulfide bonds. On cooling a solution of denatured BPTI, the activity of the protein is restored. What is the molecular basis for this property?
Formal Charges
Formal charges have an important role in organic chemistry since this concept helps us to know whether an atom in a molecule is neutral/bears a positive or negative charge. Even if some molecules are neutral, the atoms within that molecule need not be neutral atoms.
Polarity Of Water
In simple chemical terms, polarity refers to the separation of charges in a chemical species leading into formation of two polar ends which are positively charged end and negatively charged end. Polarity in any molecule occurs due to the differences in the electronegativities of the bonded atoms. Water, as we all know has two hydrogen atoms bonded to an oxygen atom. As oxygen is more electronegative than hydrogen thus, there exists polarity in the bonds which is why water is known as a polar solvent.
Valence Bond Theory Vbt
Valence bond theory (VBT) in simple terms explains how individual atomic orbitals with an unpaired electron each, come close to each other and overlap to form a molecular orbital giving a covalent bond. It gives a quantum mechanical approach to the formation of covalent bonds with the help of wavefunctions using attractive and repulsive energies when two atoms are brought from infinity to their internuclear distance.
Some natural proteins are rich in disulfide bonds, and their mechanical properties (tensile strength, viscosity, hardness, etc.) are correlated with the degree of disulfide bonding. (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 α-keratin. What is the molecular basis for the correlation between disulfide-bond content and mechanical properties of the protein?
(b) Most globular proteins are denatured and lose their activity when briefly heated to 65 °C. However, globular proteins that contain multiple disulfide bonds often must be heated longer at higher temperatures to denature them. One such protein is bovine pancreatic trypsin inhibitor (BPTI), which has 58 amino acid residues in a single chain and
contains three disulfide bonds. On cooling a solution of denatured BPTI, the activity of the protein is restored. What is the molecular basis for this property?
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