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Characterizing Domain Interfaces by NMR

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Protein NMR Techniques

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

Abstract

The combination of chemical shift, residual dipolar coupling, and backbone relaxation data can be used to characterize the nature of a domain interface in a multidomain protein. Comparison of the parameters obtained from isolated domains and domain pairs provides insight into the composition of the interface as well as into interdomain dynamics. The interface between the 13th and 14th F3 module from fibronectin is used as an example.

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Author information

Authors and Affiliations

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

    Luke M. Rooney,  Sachchidanand & Jörn M. Werner

Authors
  1. Luke M. Rooney
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  2. Sachchidanand
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  3. Jörn M. Werner
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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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Rooney, L.M., Sachchidanand, Werner, J.M. (2004). Characterizing Domain Interfaces by NMR. In: Downing, A.K. (eds) Protein NMR Techniques. Methods in Molecular Biology™, vol 278. Humana Press. https://doi.org/10.1385/1-59259-809-9:123

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  • DOI: https://doi.org/10.1385/1-59259-809-9:123

  • Publisher Name: Humana Press

  • Print ISBN: 978-1-58829-246-9

  • Online ISBN: 978-1-59259-809-0

  • eBook Packages: Springer Protocols

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