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Determination of High-resolution NMR Structures of Proteins

  • Chapter
NMR of Proteins

Part of the book series: Topics in Molecular and Structural Biology ((TMSB))

Abstract

As a result of continuing development over the past decade of increasingly sophisticated high-field NMR spectrometers and novel multidimensional experiments, NMR has emerged as a powerful method for determination of the three-dimensional structures of small proteins in solution. The first protein structures were reported in 1985 (Kaptein et al., 1985; Williamson et al., 1985) and were, not surprisingly, of relatively low resolution. Since then, intensive efforts have been directed towards development of methods for obtaining refined, high-resolution structures. In this chapter we describe our methods for structure determination and refinement, using the proteins plastocyanin, myoglobin and a zinc finger as examples. Some of our computation methods, such as distance geometry and restrained molecular dynamics, are by now relatively standard. However, refinements based on NOE intensities and chemical shifts are not yet commonplace, and we therefore describe our efforts in these directions in some detail.

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Authors
  1. David A. Case
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  2. Peter E. Wright
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Editors and Affiliations

  1. Laboratory of Chemical Physics, National Institutes of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, MD, 20892, USA

    G. M. Clore  & A. M. Gronenborn  & 

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Case, D.A., Wright, P.E. (1993). Determination of High-resolution NMR Structures of Proteins. In: Clore, G.M., Gronenborn, A.M. (eds) NMR of Proteins. Topics in Molecular and Structural Biology. Palgrave, London. https://doi.org/10.1007/978-1-349-12749-8_3

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  • DOI: https://doi.org/10.1007/978-1-349-12749-8_3

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