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Looking at macromolecular structures and dynamics with Single Molecule Förster Resonance Energy Transfer (smFRET)
Förster Resonance Energy Transfer (FRET) allows measuring the distance
between two spectrally distinct fluorophores, in the 20-100 Å range.
When monitored at the single molecule level, smFRET is useful in
resolving subpopulations, or observing conformational changes as a
function of time within single macromolecular complexes in vitro. I
will describe here the methodologies used to label biomolecules with
fluorescent dyes, and measure interprobes distances accurately on the
labelled complexes, freely diffusing in solution or immobilized on
surfaces. I will focus on the study of complexes involved in
prokaryotic transcription initiation and termination (helicases and
polymerases). Finally, I will discuss how information gathered from
smFRET experiments could be used to complement other high- or
low-resolution methods in structural biology.
Séminaires Gulliver : consulter le programme
Informations contextuelles :
Contact : mathilde.reyssat@espci.fr