Unknown

Dataset Information

0

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

altmetric image

Publications

The effect of protein composition on hydration dynamics.

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]

Similar Datasets

| S-EPMC2480692 | biostudies-literature
| S-EPMC2951393 | biostudies-other
| S-EPMC5519773 | biostudies-literature
| S-EPMC2141799 | biostudies-literature
| S-EPMC3305823 | biostudies-literature
| S-EPMC7423024 | biostudies-literature
| S-EPMC1303358 | biostudies-literature
| S-EPMC518771 | biostudies-literature
| S-EPMC9245114 | biostudies-literature
| S-EPMC6005386 | biostudies-literature