Resolving distance variations by single-molecule FRET and EPR spectroscopy using rotamer libraries.

ABSTRACT: Förster resonance energy transfer (FRET) and electron paramagnetic resonance (EPR) spectroscopy are complementary techniques for quantifying distances in the nanometer range. Both approaches are commonly employed for probing the conformations and conformational changes of biological macromolecules based on site-directed fluorescent or paramagnetic labeling. FRET can be applied in solution at ambient temperature and thus provides direct access to dynamics, especially if used at the single-molecule level, whereas EPR requires immobilization or work at cryogenic temperatures but provides data that can be more reliably used to extract distance distributions. However, a combined analysis of the complementary data from the two techniques has been complicated by the lack of a common modeling fram

SUBMITTER: Klose D 

PROVIDER: S-EPMC8595751 | biostudies-literature | 2021 Nov

REPOSITORIES: biostudies-literature