Practice question

Protease hydrolysis cleaves peptide bonds, fragmenting chain and disrupting hydrogen bonded networks that stabilize helices and sheets. Far-ultraviolet circular dichroism monitors these networks via amide n to pi-star and pi to pi-star bands; loss of distinct minima at 208, 222 or 218 nanometers and appearance of random coil signature near 195 nanometers reflects conformational alteration and unfolding of remaining fragments. Primary sequence composition change alone without structural rearrangement would not alter CD significantly; fluorescence quenching reports side chain environment, disulfide cleavage requires reductant, not protease.