Direct observation of ultrafast folding and denatured state dynamics in single protein molecules.

ABSTRACT: Single-molecule fluorescence resonance energy transfer (smFRET) experiments are extremely useful in studying protein folding but are generally limited to time scales of greater than approximately 100 micros and distances greater than approximately 2 nm. We used single-molecule fluorescence quenching by photoinduced electron transfer, detecting short-range events, in combination with fluorescence correlation spectroscopy (PET-FCS) to investigate folding dynamics of the small binding domain BBL with nanosecond time resolution. The kinetics of folding appeared as a 10-micros decay in the autocorrelation function, resulting from stochastic fluctuations between denatured and native conformations of individual molecules. The observed rate constants were probe independent and in excellent agreeme

SUBMITTER: Neuweiler H 

PROVIDER: S-EPMC2773960 | biostudies-literature | 2009 Nov

REPOSITORIES: biostudies-literature