The effect of protein composition on hydration dynamics.

ABSTRACT: Water dynamics at the surface of two homologous proteins with different thermal resistances is found to be unaffected by the different underlying amino-acid compositions, and when proteins are folded it responds similarly to temperature variations. Upon unfolding the water dynamics slowdown with respect to bulk decreases by a factor of two. Our findings are explained by the dominant topological perturbation induced by the protein on the water hydrogen bond dynamics.

SUBMITTER: Rahaman O 

PROVIDER: S-EPMC3827537 | biostudies-literature | 2013 Mar

REPOSITORIES: biostudies-literature