How accurate are polymer models in the analysis of Förster resonance energy transfer experiments on proteins?

Abstract

Single molecule Förster resonance energy transfer (FRET) experiments are used to infer the properties of the denatured state ensemble (DSE) of proteins. From the measured average FRET efficiency, <E>, the distance distribution P(R) is inferred by assuming that the DSE can be described as a polymer. The single parameter in the appropriate polymer model… (More)
DOI: 10.1063/1.3082151

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@article{OBrien2009HowAA, title={How accurate are polymer models in the analysis of F{\"{o}rster resonance energy transfer experiments on proteins?}, author={Edward P O'Brien and Greg Morrison and Bernard R. Brooks and D. Thirumalai}, journal={The Journal of chemical physics}, year={2009}, volume={130 12}, pages={124903} }