Site-specific hydration dynamics in the nonpolar core of a molten globule by dynamic nuclear polarization of water.

ABSTRACT: Water-protein interactions play a direct role in protein folding. The chain collapse that accompanies protein folding involves extrusion of water from the nonpolar core. For many proteins, including apomyoglobin (apoMb), hydrophobic interactions drive an initial collapse to an intermediate state before folding to the final structure. However, the debate continues as to whether the core of the collapsed intermediate state is hydrated and, if so, what the dynamic nature of this water is. A key challenge is that protein hydration dynamics is significantly heterogeneous, yet suitable experimental techniques for measuring hydration dynamics with site-specificity are lacking. Here, we introduce Overhauser dynamic nuclear polarization at 0.35 T via site-specific nitroxide spin labels as a unique

SUBMITTER: Armstrong BD 

PROVIDER: S-EPMC3095581 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature