Compressibility and Volume Changes of Lysozyme Due to Guanidine Hydrochloride Denaturation

Abstract

Abstract The apparent specific volume and adiabatic compressibility of lysozyme largely decreased upon guanidine hydrochloride denaturation. These results demonstrate that a large amount of amino acid residues exposes accompanying an increase in hydration and a decrease in the internal cavity. Both parameters deviated from the two-state transition curves, suggesting noncooperative disruption of the compactness and the secondary structure.