Hydration studies on the archaeal protein Sso7d using NMR measurements and MD simulations.

ABSTRACT:

Background

How proteins approach surrounding molecules is fundamental to our understanding of the specific interactions that occur at the surface of proteins. The enhanced surface accessibility of small molecules such as organic solvents and paramagnetic probes to protein binding sites has been observed; however, the molecular basis of this finding has not been fully established. Recently, it has been suggested that hydration dynamics play a predominant role in controlling the distribution of hot spots on surface of proteins.

Results

In the present study, the hydration of the archaeal multifunctional protein Sso7d from Solfolobus solfataricus was investigated using a combination of computational and experimental data derived from molecular dynamics simulations and ePHOGSY NM

SUBMITTER: Bernini A 

PROVIDER: S-EPMC3207888 | biostudies-literature | 2011 Oct

REPOSITORIES: biostudies-literature