Govt. Exams
Entrance Exams
Extreme pH causes ionization of amino acid side chains and disruption of protein structure, leading to denaturation and loss of enzymatic activity.
Quaternary structure involves interactions between different polypeptide chains, not covalent peptide bonds. Only non-covalent interactions maintain quaternary structure.
Leucine, Isoleucine, and Valine are branched-chain hydrophobic amino acids typically buried in the interior of folded proteins.
Peptide bond formation is part of protein synthesis and structure, not denaturation. Denaturation involves disruption of secondary and tertiary structures.
In competitive inhibition, the inhibitor competes with substrate for the active site and can be overcome by increasing substrate concentration.
Km (Michaelis constant) represents the substrate concentration at which enzyme velocity is half of Vmax, indicating substrate affinity.
Serine is an amino acid, not a cofactor. Cofactors include metal ions and coenzymes like NAD⁺, FAD, and CoA.
