Journal
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
Volume 15, Issue 10, Pages 3570-3576Publisher
ROYAL SOC CHEMISTRY
DOI: 10.1039/c3cp44582h
Keywords
-
Funding
- European Research Council [258748]
- CINECA ISCRA [KINPROT HP10B86HLY, FLEXPROT HP10BTJ4LQ]
- European Research Council (ERC) [258748] Funding Source: European Research Council (ERC)
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available