Defining a length scale for millisecond-timescale protein conformational exchange.

ABSTRACT: Although atomic resolution 3D structures of protein native states and some folding intermediates are available, the mechanism of interconversion between such states remains poorly understood. Here we study the four-helix bundle FF module, which folds via a transiently formed and sparsely populated compact on-pathway intermediate, I. Relaxation dispersion NMR spectroscopy has previously been used to elucidate the 3D structure of this intermediate and to establish that the conformational exchange between the I and the native, N, states of the FF domain is driven predominantly by water dynamics. In the present study we use NMR methods to define a length scale for the FF I-N transition, namely the effective hydrodynamic radius (EHR) that provides an average measure of the size of the structura

SUBMITTER: Sekhar A 

PROVIDER: S-EPMC3710843 | biostudies-literature | 2013 Jul

REPOSITORIES: biostudies-literature