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Protein Structural Dynamics Revealed by Site-Directed Spin Labeling and Multifrequency EPR

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Protein Dynamics

Part of the book series: Methods in Molecular Biology ((MIMB,volume 1084))

Abstract

Multifrequency electron paramagnetic resonance (EPR) of spin-labeled protein is a powerful spectroscopic technique to study protein dynamics on the rotational correlation time scale from 100 ps to 100 ns. Nitroxide spin probe, attached to cysteine residue, reports on local topology within the labeling site, dynamics of protein domains reorientation, and protein global tumbling in solution. Due to spin probe’s magnetic tensors anisotropy, its mobility is directly reflected by the EPR lineshape. The multifrequency approach significantly decreases ambiguity of EPR spectra interpretation. The approach, described in this chapter, provides a practical guideline that can be followed to carry out the experiments and data analysis.

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Acknowledgements

This work was supported by NIH grants AR53562, AR59621. NLSL and NLSL-SRLS software was kindly provided by Dr. Z. Liang and Dr. J.H. Freed (Cornell University).

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Authors and Affiliations

  1. Department of Physics and Optical Science, University of North Carolina at Charlotte, Charlotte, NC, USA

    Yuri E. Nesmelov

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  1. Yuri E. Nesmelov
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Editors and Affiliations

  1. Department of Bioinformatics and Genomic, University of North Carolina at Charlott, Charlotte, North Carolina, USA

    Dennis R. Livesay

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Nesmelov, Y.E. (2014). Protein Structural Dynamics Revealed by Site-Directed Spin Labeling and Multifrequency EPR. In: Livesay, D. (eds) Protein Dynamics. Methods in Molecular Biology, vol 1084. Humana Press, Totowa, NJ. https://doi.org/10.1007/978-1-62703-658-0_4

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  • DOI: https://doi.org/10.1007/978-1-62703-658-0_4

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  • Publisher Name: Humana Press, Totowa, NJ

  • Print ISBN: 978-1-62703-657-3

  • Online ISBN: 978-1-62703-658-0

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