The mechanism by which urea and guanidinium destabilize protein structure is controversial. We tested the possibility that these denaturants form hydrogen bonds with peptide groups by measuring their ability to block acid- and base-catalyzed peptide hydrogen exchange. The peptide hydrogen bonding found appears sufficient to explain the thermodynamic denaturing effect of urea. Results for guanidinium, however, are contrary to the expectation that it might H-bond. Evidently, urea and guanidinium, although structurally similar, denature proteins by different mechanisms.
机构:
Univ Calif Santa Barbara, Dept Chem & Biochem, Santa Barbara, CA 93106 USAUniv Calif Santa Barbara, Dept Chem & Biochem, Santa Barbara, CA 93106 USA
Ganguly, Pritam
Shea, Joan-Emma
论文数: 0引用数: 0
h-index: 0
机构:
Univ Calif Santa Barbara, Dept Chem & Biochem, Santa Barbara, CA 93106 USA
Univ Calif Santa Barbara, Dept Phys, Santa Barbara, CA 93106 USAUniv Calif Santa Barbara, Dept Chem & Biochem, Santa Barbara, CA 93106 USA