Accounting for fast vs slow exchange in single molecule FRET experiments reveals hidden conformational states.

ABSTRACT: Proteins are dynamic systems whose structural preferences determine their function. Unfortunately, building atomically detailed models of protein structural ensembles remains challenging, limiting our understanding of the relationships between sequence, structure, and function. Combining single molecule Förster resonance energy transfer (smFRET) experiments with molecular dynamics simulations could provide experimentally grounded, all-atom models of a protein's structural ensemble. However, agreement between the two techniques is often insufficient to achieve this goal. Here, we explore whether accounting for important experimental details like averaging across structures sampled during a given smFRET measurement is responsible for this apparent discrepancy. We present an approach to accou

SUBMITTER: Miller JJ 

PROVIDER: S-EPMC11185552 | biostudies-literature | 2024 Jun

REPOSITORIES: biostudies-literature