Cooperative water filling of a nonpolar protein cavity observed by high-pressure crystallography and simulation.

ABSTRACT: Formation of a water-expelling nonpolar core is the paradigm of protein folding and stability. Although experiment largely confirms this picture, water buried in "hydrophobic" cavities is required for the function of some proteins. Hydration of the protein core has also been suggested as the mechanism of pressure-induced unfolding. We therefore are led to ask whether even the most nonpolar protein core is truly hydrophobic (i.e., water-repelling). To answer this question we probed the hydration of an approximately 160-A(3), highly hydrophobic cavity created by mutation in T4 lysozyme by using high-pressure crystallography and molecular dynamics simulation. We show that application of modest pressure causes approximately four water molecules to enter the cavity while the protein itself rema

SUBMITTER: Collins MD 

PROVIDER: S-EPMC1283839 | biostudies-literature | 2005 Nov

REPOSITORIES: biostudies-literature