Protein Structure and Dynamics from Single-Molecule Fluorescence Resonance Energy Transfer
- 8 January 2005
- journal article
- research article
- Published by American Chemical Society (ACS) in The Journal of Physical Chemistry B
- Vol. 109 (4), 1626-1634
- https://doi.org/10.1021/jp0478864
Abstract
The pros and cons of single-molecule vs ensemble-averaged fluorescence resonance energy transfer (FRET) experiments, performed on proteins, are explored with the help of Langevin dynamics simulations. An off-lattice model of the polypeptide chain is employed, which gives rise to a well-defined native state and two-state folding kinetics. A detailed analysis of the distribution of the donor-acceptor distance is presented at different points along the denaturation curve, along with its dependence on the averaging time window. We show that unique information on the correlation between structure and dynamics, which can only be obtained from single-molecule experiments, is contained in the correlation between the donor-acceptor distance and its displacement. The latter is shown to provide useful information on the free energy landscape of the protein, which is complementary to that obtained from the distribution of donor-acceptor distances.Keywords
This publication has 50 references indexed in Scilit:
- Single-Macromolecule Fluorescence Resonance Energy Transfer and Free-Energy ProfilesThe Journal of Physical Chemistry B, 2003
- FRET by FET and Dynamics of Polymer FoldingThe Journal of Physical Chemistry B, 2001
- Determination of intramolecular distance distribution during protein folding on the millisecond timescaleJournal of Molecular Biology, 2000
- Ratiometric Analysis of Single-Molecule Fluorescence Resonance Energy Transfer Using Logical Combinations of Threshold Criteria: A Study of 12-mer DNAThe Journal of Physical Chemistry B, 2000
- Hydrophobic Interactions in Aqueous Urea Solutions with Implications for the Mechanism of Protein DenaturationJournal of the American Chemical Society, 1998
- Viscosity Dependence of the Folding Rates of ProteinsPhysical Review Letters, 1997
- Probing the interaction between two single molecules: fluorescence resonance energy transfer between a single donor and a single acceptor.Proceedings of the National Academy of Sciences, 1996
- Kinetic and thermodynamic analysis of proteinlike heteropolymers: Monte Carlo histogram techniqueThe Journal of Chemical Physics, 1995
- Folding kinetics of proteinlike heteropolymersThe Journal of Chemical Physics, 1994
- Zwischenmolekulare Energiewanderung und FluoreszenzAnnalen der Physik, 1948