Issue 10, 2013

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.

Graphical abstract: The effect of protein composition on hydration dynamics

Supplementary files

Article information

Article type
Paper
Submitted
18 Dec 2012
Accepted
07 Jan 2013
First published
10 Jan 2013

Phys. Chem. Chem. Phys., 2013,15, 3570-3576

The effect of protein composition on hydration dynamics

O. Rahaman, S. Melchionna, D. Laage and F. Sterpone, Phys. Chem. Chem. Phys., 2013, 15, 3570 DOI: 10.1039/C3CP44582H

To request permission to reproduce material from this article, please go to the Copyright Clearance Center request page.

If you are an author contributing to an RSC publication, you do not need to request permission provided correct acknowledgement is given.

If you are the author of this article, you do not need to request permission to reproduce figures and diagrams provided correct acknowledgement is given. If you want to reproduce the whole article in a third-party publication (excluding your thesis/dissertation for which permission is not required) please go to the Copyright Clearance Center request page.

Read more about how to correctly acknowledge RSC content.

Social activity

Spotlight

Advertisements