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Application of Single Molecule Förster Resonance Energy Transfer to Protein Folding

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Protein Folding Protocols

Part of the book series: Methods in Molecular Biology™ ((MIMB,volume 350))

Abstract

Protein folding is a process characterized by a large degree of conformational heterogeneity. In such cases, classical experimental methods yield only mean values, averaged over large ensembles of molecules. The microscopic distributions of conformations, trajectories, or sequences of events often remain unknown, and with them the underlying molecular mechanisms. Signal averaging can be avoided by observing individual molecules. A particularly versatile method is highly sensitive fluorescence detection. In combination with Förster resonance energy transfer, distances and conformational dynamics can be investigated in single molecules. This chapter introduces the practical aspects of applying this method to protein folding.

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Authors and Affiliations

  1. Department of Biochemistry, University of Zürich, Zürich, Switzerland

    Benjamin Schuler

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  1. Benjamin Schuler
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Editors and Affiliations

  1. Laboratory of Biochemistry, National Cancer Institute, National Institutes of Health, Bethesda, MD

    Yawen Bai

  2. Center for Cancer Research Nanobiology Program SAIC, National Cancer Institute-Frederick, Frederick, MD

    Ruth Nussinov

  3. Department of Human Genetics, Sackler School of Medicine, Tel Aviv University, Tel Aviv, Israel

    Ruth Nussinov

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© 2007 Humana Press Inc.

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Schuler, B. (2007). Application of Single Molecule Förster Resonance Energy Transfer to Protein Folding. In: Bai, Y., Nussinov, R. (eds) Protein Folding Protocols. Methods in Molecular Biology™, vol 350. Humana Press. https://doi.org/10.1385/1-59745-189-4:115

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  • DOI: https://doi.org/10.1385/1-59745-189-4:115

  • Publisher Name: Humana Press

  • Print ISBN: 978-1-58829-622-1

  • Online ISBN: 978-1-59745-189-5

  • eBook Packages: Springer Protocols

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