BIOMOLECULES AND ENZYMES

Detailed explanation-1: -A protein becomes denatured when its normal shape gets deformed because some of the hydrogen bonds are broken. Weak hydrogen bonds break when too much heat is applied or when they are exposed to an acid (like citric acid from lemon juice).

Detailed explanation-2: -Heat can be used to disrupt hydrogen bonds and non-polar hydrophobic interactions. This occurs because heat increases the kinetic energy and causes the molecules to vibrate so rapidly and violently that the bonds are disrupted.

Detailed explanation-3: -In denaturation, the peptide bonds are not affected, but the H-bonds, disulfide bonds, salt bridges and hydrophobic interactions can all be disrupted, leading to the consecutive alteration of 4o, 3o and 2o structure.

Detailed explanation-4: -Secondary structure The most common types of secondary structures are the helix and the pleated sheet. Both structures are held in shape by hydrogen bonds, which form between the carbonyl O of one amino acid and the amino H of another.

Detailed explanation-5: -Primary structure, such as the sequence of amino acids held together by covalent peptide bonds, is not disrupted by denaturation.