Answer: Loss of 3D structure without breaking peptide bonds.
- A Hydrolytic cleavage of the covalent peptide bonds linking amino acid residues
- B Loss of 3D structure without breaking peptide bonds
- C Condensation reactions forming additional peptide bonds within the chain
- D De novo synthesis of new amino acid monomers from precursor molecules
Correct answer: B. Loss of 3D structure without breaking peptide bonds
Explanation: Denaturation disrupts secondary and tertiary structure (breaking H bonds, hydrophobic interactions, disulfide bonds) but does NOT break peptide bonds of the primary structure.
As substrate concentration rises, reaction rate increases steeply at first, then plateaus at Vmax once every enzyme molecule is working at full capacity; Km is the substrate concentration giving half-maximal rate, and a LOWER Km means the enzyme reaches that rate with less substrate (higher affinity).
Concept context
Carbohydrates, proteins, lipids, nucleic acids, and enzyme kinetics. Essential foundation for understanding metabolism.