Time-resolved structural studies of protein reaction dynamics: a smorgasbord of X-ray approaches.

ABSTRACT: Proteins undergo conformational changes during their biological function. As such, a high-resolution structure of a protein's resting conformation provides a starting point for elucidating its reaction mechanism, but provides no direct information concerning the protein's conformational dynamics. Several X-ray methods have been developed to elucidate those conformational changes that occur during a protein's reaction, including time-resolved Laue diffraction and intermediate trapping studies on three-dimensional protein crystals, and time-resolved wide-angle X-ray scattering and X-ray absorption studies on proteins in the solution phase. This review emphasizes the scope and limitations of these complementary experimental approaches when seeking to understand protein conformational dynamics

SUBMITTER: Westenhoff S 

PROVIDER: S-EPMC2824530 | biostudies-literature | 2010 Mar

REPOSITORIES: biostudies-literature