Govt Exams
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.
Hemoglobin is a globular protein with a compact, spherical structure, unlike fibrous proteins like collagen and keratin.
At isoelectric point, the number of positive charges equals negative charges, resulting in zero net charge and minimum solubility.
Carboxypeptidase is an exopeptidase that removes amino acids sequentially from the C-terminal end of proteins.
Peptide bonds between the carboxyl group of one amino acid and the amino group of the next maintain the primary structure.
Selenocysteine is the 21st amino acid and is not among the standard 20 protein amino acids. It contains selenium instead of sulfur.