Accuracy of distance distributions and dynamics from single-molecule FRET.

ABSTRACT: Single-molecule spectroscopy combined with Förster resonance energy transfer is widely used to quantify distance dynamics and distributions in biomolecules. Most commonly, measurements are interpreted using simple analytical relations between experimental observables and the underlying distance distributions. However, these relations make simplifying assumptions, such as a separation of timescales between interdye distance dynamics, fluorescence lifetimes, and dye reorientation, the validity of which is notoriously difficult to assess from experimental data alone. Here, we use experimentally validated long-timescale, all-atom explicit-solvent molecular dynamics simulations of a disordered peptide with explicit fluorophores for testing these assumptions, in particular the separation of the

SUBMITTER: Nuesch M 

PROVIDER: S-EPMC12709264 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature