Mapping protein conformational heterogeneity under pressure with site-directed spin labeling and double electron-electron resonance.

ABSTRACT: The dominance of a single native state for most proteins under ambient conditions belies the functional importance of higher-energy conformational states (excited states), which often are too sparsely populated to allow spectroscopic investigation. Application of high hydrostatic pressure increases the population of excited states for study, but structural characterization is not trivial because of the multiplicity of states in the ensemble and rapid (microsecond to millisecond) exchange between them. Site-directed spin labeling in combination with double electron-electron resonance (DEER) provides long-range (20-80 Å) distance distributions with angstrom-level resolution and thus is ideally suited to resolve conformational heterogeneity in an excited state populated under high pressure. D

SUBMITTER: Lerch MT 

PROVIDER: S-EPMC3977274 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature