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NMR Approaches to Protein Structure and Function

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Neurotox ’91

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Abstract

The revolution in NMR techniques over the last few years has enormously increased the power of NMR spectroscopy for the study of protein structure and interactions in solution. Three-dimensional structures of small proteins can be determined, and information on structure and dynamics, and on interactions with small molecules, obtained for considerably larger proteins. The barrier represented by the complexity of 1HNMR spectra of proteins is gradually being eroded by the development of multidimensional NMR experiments and the use of isotope labelling with 2H, 13C and 15N. The latter, together with the provision of the fairly substantial quantities of protein (tens of milligrams) required for NMR spectroscopy, has been greatly facilitated by the developments in molecular genetics and the ability to construct over-expression systems. In this paper I shall briefly outline some of these applications of NMR, illustrating them primarily with examples from our own recent work. A number of reviews are available which give further details of the methodology and a broader view of the wide range of biological applications.1–6

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Authors and Affiliations

  1. Department of Biochemistry & Biological NMR Centre, University of Leicester, Leicester, LE1 9HN, UK

    Gordon C. K. Roberts

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  1. Gordon C. K. Roberts
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Editors and Affiliations

  1. Department of Life Science, University of Nottingham, University Park, NG7 2RD, Nottingham, UK

    I. R. Duce

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Roberts, G.C.K. (1992). NMR Approaches to Protein Structure and Function. In: Duce, I.R. (eds) Neurotox ’91. Springer, Dordrecht. https://doi.org/10.1007/978-94-011-2898-8_16

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  • DOI: https://doi.org/10.1007/978-94-011-2898-8_16

  • Publisher Name: Springer, Dordrecht

  • Print ISBN: 978-1-85166-746-8

  • Online ISBN: 978-94-011-2898-8

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