Protein surface hydration mapped by site-specific mutations.

ABSTRACT: Water motion at protein surfaces is fundamental to protein structure, stability, dynamics, and function. By using intrinsic tryptophans as local optical probes, and with femtosecond resolution, it is possible to probe surface-water motions in the hydration layer. Here, we report our studies of local hydration dynamics at the surface of the enzyme Staphylococcus nuclease using site-specific mutations. From these studies of the WT and four related mutants, which change local charge distribution and structure, we are able to ascertain the contribution to solvation by protein side chains as relatively insignificant. We determined the time scales of hydration to be 3-5 ps and 100-150 ps. The former is the result of local librational/rotational motions of water near the surface; the latter is a

SUBMITTER: Qiu W 

PROVIDER: S-EPMC1599899 | biostudies-literature | 2006 Sep

REPOSITORIES: biostudies-literature