Step 1: Understanding protein denaturation.
Protein denaturation refers to the process where the native structure of a protein is disrupted, typically due to physical or chemical changes such as heat, pH alterations, or chemical treatments. Denaturation affects the secondary, tertiary, and quaternary structures, but does not break the primary structure (peptide bonds).
Step 2: Analyzing the options.
- (A) Correct, denaturation can lead to an increase in \(\alpha\)-helix and \(\beta\)-sheet structures, but these structures become less organized and more random.
- (B) Incorrect, denaturation is often reversible under certain conditions. For example, proteins can refold back to their native state after denaturation if the denaturing agent is removed.
- (C) Correct, fully denatured globular proteins typically lose their native three-dimensional structure and resemble a random coil, lacking any specific secondary or tertiary structure.
- (D) Incorrect, the peptide bonds themselves are not broken during denaturation. Denaturation affects higher-order structures but does not cleave the covalent peptide bonds.
Step 3: Conclusion.
Thus, the correct answers are (A) and (C).