A Quantitative Theoretical Framework For Protein-Induced Fluorescence Enhancement-Forster-Type Resonance Energy Transfer (PIFE-FRET).

ABSTRACT: Single-molecule, protein-induced fluorescence enhancement (PIFE) serves as a molecular ruler at molecular distances inaccessible to other spectroscopic rulers such as Förster-type resonance energy transfer (FRET) or photoinduced electron transfer. In order to provide two simultaneous measurements of two distances on different molecular length scales for the analysis of macromolecular complexes, we and others recently combined measurements of PIFE and FRET (PIFE-FRET) on the single molecule level. PIFE relies on steric hindrance of the fluorophore Cy3, which is covalently attached to a biomolecule of interest, to rotate out of an excited-state trans isomer to the cis isomer through a 90° intermediate. In this work, we provide a theoretical framework that accounts for relevant photophysical

SUBMITTER: Lerner E 

PROVIDER: S-EPMC4939467 | biostudies-literature | 2016 Jul

REPOSITORIES: biostudies-literature