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Heteronuclear NMR Studies of the Molecular Dynamics of Staphylococcal Nuclease

  • Chapter
NMR of Proteins

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

Abstract

During the past decade tremendous progress has been made in developing NMR techniques to determine the structure of proteins in solution. For proteins containing less than c. 100 residues, essentially complete proton signal assignments can be obtained using two- and three-dimensional homonuclear (proton) pulse sequences (Wüthrich, 1986; Clore and Gronenborn, 1989). These assignments together with distance and dihedral angle constraints, derived from NOEs and coupling constants, respectively, provide sufficient information to determine the three-dimensional structure of the protein. Recently it has been shown that NMR methods can be applied to larger proteins, containing up to c. 200 residues, by combining heteronuclear labelling (with 13C and/or 15N) with sophisticated double- and triple-resonance multidimensional techniques (Bax et al., 1990; Fesik et al., 1990; Ikura et al., 1990; Kay et al., 1990a,b; Clore et al., 1991a,b; Pelton et al., 1991).

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Authors
  1. Dennis A. Torchia
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  2. Linda K. Nicholson
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  3. Holly B. R. Cole
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  4. Lewis E. Kay
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Editor information

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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Torchia, D.A., Nicholson, L.K., Cole, H.B.R., Kay, L.E. (1993). Heteronuclear NMR Studies of the Molecular Dynamics of Staphylococcal Nuclease. 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_7

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  • DOI: https://doi.org/10.1007/978-1-349-12749-8_7

  • Publisher Name: Palgrave, London

  • Print ISBN: 978-1-349-12751-1

  • Online ISBN: 978-1-349-12749-8

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