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Calculating Protein Structures from NMR Data

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Protein NMR Techniques

Part of the book series: Methods in Molecular Biology™ ((MIMB,volume 60))

Abstract

Today many, if not most, NMR measurements with proteins are performed with the ultimate aim of determining their three-dimensional (3D) structure (1). However, NMR is not a “microscope with atomic resolution” that would directly produce an image of a protein. Rather, it is able to yield a wealth of indirect structural information from which the 3D structure can be revealed only by extensive calculations. The pioneering first structure determinations of proteins in solution (e.g., 2–6) were year-long struggles, both fascinating and tedious because of the lack of established NMR techniques and numerical methods for structure calculation, and hampered by limitations of the spectrometers and computers of the time. Recent experimental, theoretical, and technological advances —and the dissemination of the methodological knowledge—have changed this situation completely: Given a sufficient amount of a purified, water-soluble protein with less than approx 200 amino acid residues, its 3D structure in solution can be determined routinely by the NMR method. Protein structures with up to about 100 residues can be solved by [1H]-NMR alone, whereas for larger proteins labeling with 13C and 15N is required.

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  1. Institute for Molecular Biology and Biophysics, Zurich, Switzerland

    Peter Güntert

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  1. Peter Güntert
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  1. SmithKline Beecham Pharmaceuticals, Welwyn, Hertfordshire, UK

    David G. Reid

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© 1997 Humana Press Inc.

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Güntert, P. (1997). Calculating Protein Structures from NMR Data. In: Reid, D.G. (eds) Protein NMR Techniques. Methods in Molecular Biology™, vol 60. Humana Press. https://doi.org/10.1385/0-89603-309-0:157

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  • DOI: https://doi.org/10.1385/0-89603-309-0:157

  • Publisher Name: Humana Press

  • Print ISBN: 978-0-89603-309-2

  • Online ISBN: 978-1-59259-546-4

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