Structures of invisible, excited protein states by relaxation dispersion NMR spectroscopy.

ABSTRACT: Molecular function is often predicated on excursions between ground states and higher energy conformers that can play important roles in ligand binding, molecular recognition, enzyme catalysis, and protein folding. The tools of structural biology enable a detailed characterization of ground state structure and dynamics; however, studies of excited state conformations are more difficult because they are of low population and may exist only transiently. Here we describe an approach based on relaxation dispersion NMR spectroscopy in which structures of invisible, excited states are obtained from chemical shifts and residual anisotropic magnetic interactions. To establish the utility of the approach, we studied an exchanging protein (Abp1p SH3 domain)-ligand (Ark1p peptide) system, in which th

SUBMITTER: Vallurupalli P 

PROVIDER: S-EPMC2575287 | biostudies-literature | 2008 Aug

REPOSITORIES: biostudies-literature