Extracting rate coefficients from single-molecule photon trajectories and FRET efficiency histograms for a fast-folding protein.

ABSTRACT: Recently developed statistical methods by Gopich and Szabo were used to extract folding and unfolding rate coefficients from single-molecule Förster resonance energy transfer (FRET) data for proteins with kinetics too fast to measure waiting time distributions. Two types of experiments and two different analyses were performed. In one experiment bursts of photons were collected from donor and acceptor fluorophores attached to a 73-residue protein, α(3)D, freely diffusing through the illuminated volume of a confocal microscope system. In the second, the protein was immobilized by linkage to a surface, and photons were collected until one of the fluorophores bleached. Folding and unfolding rate coefficients and mean FRET efficiencies for the folded and unfolded subpopulations were obtained f

SUBMITTER: Chung HS 

PROVIDER: S-EPMC6407426 | biostudies-literature | 2011 Apr

REPOSITORIES: biostudies-literature