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Measuring conformational dynamics of biomolecules by single molecule fluorescence spectroscopy

Nature Structural Biology volume 7, pages 724–729 (2000)Cite this article

Abstract

Dynamic structural changes of macromolecules undergoing biochemical reactions can be studied using novel single molecule spectroscopy tools. Recent advances in applying such distance and orientation molecular rulers to biological systems are reviewed, and future prospects and challenges are discussed.

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Figure 1: Energy landscape for the folding reaction.
Figure 2: Single molecule protein folding.
Figure 3: Single molecule ribozyme folding.
Figure 4: Single molecule dipole rotation.
Figure 5: Single pair FRET in a living cell.

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Acknowledgements

The author is indebted to A.P. Alivisatos, U. Banin, M. Bruchez, D.S. Chemla, M. Dahan, A.A. Deniz, Th. Enderle, J. Glass, J. Grunwell, T. Ha, T. Her, Th. Lacoste, T. Laurence, J. Liang, S. Licht, A. B. Martin, X. Michalet, F. Pinaud, P.G. Schultz, P.R. Selvin, A. Sonnleitner, and A.Y. Ting for their contributions to the single molecule spectroscopy effort in Berkeley and to A.A. Deniz, T. Her and X. Michalet for critical reading of the manuscript. This work was supported by the Laboratory Directed Research and Development Program of Lawrence Berkeley National Laboratory and the Director, Office of Science, Office of Biological and Environmental Research, of the U.S. Department of Energy and the Office of Naval Research.

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  1. Materials Sciences and Physical Biosciences Divisions, Lawrence Berkeley National Laboratory, Berkeley, 94720, California, USA

    Shimon Weiss

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Weiss, S. Measuring conformational dynamics of biomolecules by single molecule fluorescence spectroscopy. Nat Struct Mol Biol 7, 724–729 (2000). https://doi.org/10.1038/78941

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