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Two-dimensional fluorescence resonance energy transfer as a probe for protein folding: A theoretical study

Ting, Christina L. and Makarov, Dmitrii E. (2008) Two-dimensional fluorescence resonance energy transfer as a probe for protein folding: A theoretical study. Journal of Chemical Physics, 128 (11). Art. No. 115102. ISSN 0021-9606. doi:10.1063/1.2835611.

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We describe a two-dimensional (2D), four-color fluorescence resonance energy transfer (FRET) scheme, in which the conformational dynamics of a protein is followed by simultaneously observing the FRET signal from two different donor-acceptor pairs. For a general class of models that assume Markovian conformational dynamics, we relate the properties of the emission correlation functions to the rates of elementary kinetic steps in the model. We further use a toy folding model that treats proteins as chains with breakable cross-links to examine the relationship between the cooperativity of folding and FRET data and to establish what additional information about the folding dynamics can be gleaned from 2D, as opposed to one-dimensional FRET experiments. We finally discuss the potential advantages of the four-color FRET over the three-color FRET technique.

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Additional Information:©2008 American Institute of Physics. Received 29 October 2007; accepted 26 December 2007; published 17 March 2008. We are grateful to Rick Russell, Ben Schuler, and Haw Yang, for helpful discussions. This work was supported by the National Science Foundation (Grant No. CHE 0347862) and the Robert A. Welch Foundation (Grant No. F-1514).
Subject Keywords:fluorescence, Markov processes, molecular biophysics, proteins
Issue or Number:11
Record Number:CaltechAUTHORS:TINjcp08
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Usage Policy:No commercial reproduction, distribution, display or performance rights in this work are provided.
ID Code:10096
Deposited By: Archive Administrator
Deposited On:12 Apr 2008
Last Modified:08 Nov 2021 21:05

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