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Protein NMR Techniques pp 107–122Cite as

Projection Angle Restraints for Studying Structure and Dynamics of Biomolecules

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Part of the book series: Methods in Molecular Biology™ ((MIMB,volume 278))

Abstract

This chapter presents a methodology that allows for the structural and dynamic characterization of biomolecules by means of projection restraints obtained from residual magnetic dipolar couplings. Dipolar couplings reflect the projection of individual internuclear vectors onto the alignment tensor. This technique allows determination of the dynamics of the protein backbone on time-scales, namely, between the rotational tumbling correlation time and approx 50 µs. This range of time-scales has been previously inaccessible by other nuclear magnetic resonance (NMR) techniques. In addition, information about the anisotropy of the motion is obtained.

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Author information

Authors and Affiliations

  1. Max Planck Institute for Biophysical Chemistry, Göttingen, Germany

    Christian Griesinger

  2. Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA

    Wolfgang Peti

  3. Department of Molecular Biochemistry, University of Washington, Seattle, WA

    Jens Meiler

  4. Gustaf H. Carlson School of Chemistry and Biochemistry, Clark University, Worcester, MA

    Rafael Brüschweiler

Authors
  1. Christian Griesinger
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  2. Wolfgang Peti
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  3. Jens Meiler
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  4. Rafael Brüschweiler
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Editor information

Editors and Affiliations

  1. Department of Biochemistry, University of Oxford, Oxford, UK

    A. Kristina Downing

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© 2004 Humana Press Inc., Totowa, NJ

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Griesinger, C., Peti, W., Meiler, J., Brüschweiler, R. (2004). Projection Angle Restraints for Studying Structure and Dynamics of Biomolecules. In: Downing, A.K. (eds) Protein NMR Techniques. Methods in Molecular Biology™, vol 278. Humana Press. https://doi.org/10.1385/1-59259-809-9:107

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  • DOI: https://doi.org/10.1385/1-59259-809-9:107

  • Publisher Name: Humana Press

  • Print ISBN: 978-1-58829-246-9

  • Online ISBN: 978-1-59259-809-0

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