Light-scattering studies of protein solutions: role of hydration in weak protein-protein interactions.

ABSTRACT: We model the hydration contribution to short-range electrostatic/dispersion protein interactions embodied in the osmotic second virial coefficient, B(2), by adopting a quasi-chemical description in which water molecules associated with the protein are identified through explicit molecular dynamics simulations. These water molecules reduce the surface complementarity of highly favorable short-range interactions, and therefore can play an important role in mediating protein-protein interactions. Here we examine this quasi-chemical view of hydration by predicting the interaction part of B(2) and comparing our results with those derived from light-scattering measurements of B(2) for staphylococcal nuclease, lysozyme, and chymotrypsinogen at 25 degrees C as a function of solution pH and ionic s

SUBMITTER: Paliwal A 

PROVIDER: S-EPMC1366661 | biostudies-literature | 2005 Sep

REPOSITORIES: biostudies-literature