Ontology highlight
ABSTRACT:
SUBMITTER: Rahaman O
PROVIDER: S-EPMC3827537 | biostudies-literature | 2013 Mar
REPOSITORIES: biostudies-literature
Rahaman O O Melchionna S S Laage D D Sterpone F F
Physical chemistry chemical physics : PCCP 20130204 10
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. ...[more]