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Solid-State NMR Spectroscopy of Proteins

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Biological Magnetic Resonance

Part of the book series: Biological Magnetic Resonance ((BIMR,volume 9))

Abstract

The methods and theories of solid-state NMR spectroscopy make it possible to study larger and more complex biological systems than with conventional NMR methods. They are also capable of providing unique information about the structure and dynamics of proteins. There are now a number of books and reviews that describe in detail solid-state NMR spectroscopy (e.g., Haeberlen, 1976; Mehring, 1983; Fyfe, 1983) and its applications to proteins (e.g., Oldfield et al, 1982; Torchia, 1984; Opella 1986; Opella et al, 1987).

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Author information

Authors and Affiliations

  1. Department of Chemistry, University of Pennsylvania, Phildelphia, Pennsylvania, 19104, USA

    Stanley J. Opella

Authors
  1. Stanley J. Opella
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Editor information

Editors and Affiliations

  1. Ohio State University, Columbus, Ohio, USA

    Lawrence J. Berliner

  2. Hercules Incorporated, Research Center, Wilmington, Delaware, USA

    Jacques Reuben

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© 1990 Plenum Press, New York

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Opella, S.J. (1990). Solid-State NMR Spectroscopy of Proteins. In: Berliner, L.J., Reuben, J. (eds) Biological Magnetic Resonance. Biological Magnetic Resonance, vol 9. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-6549-9_5

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  • DOI: https://doi.org/10.1007/978-1-4615-6549-9_5

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4615-6551-2

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