Protein structural dynamics revealed by site-directed spin labeling and multifrequency EPR.

ABSTRACT: Multifrequency electron paramagnetic resonance (EPR), combined with site-directed spin labeling, is a powerful spectroscopic tool to characterize protein dynamics. The lineshape of an EPR spectrum reflects combined rotational dynamics of the spin probe's local motion within a protein, reorientations of protein domains, and overall protein tumbling. All these motions can be restricted and anisotropic, and separation of these motions is important for thorough characterization of protein dynamics. Multifrequency EPR distinguishes between different motions of a spin-labeled protein, due to the frequency dependence of EPR resolution to fast and slow motion of a spin probe. This gives multifrequency EPR its unique capability to characterize protein dynamics in great detail. In this review, we an

SUBMITTER: Nesmelov YE 

PROVIDER: S-EPMC3115708 | biostudies-literature | 2010 May

REPOSITORIES: biostudies-literature