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The Folding, Stability and Dynamics of T4 Lysozyme: A Perspective Using Nuclear Magnetic Resonance

  • Chapter
NMR of Proteins

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

Abstract

In general, the primary amino acid sequence of a polypeptide chain is thought to encode all the information necessary to determine the final folded structure of a protein. However, the contributions made by individual amino acid residues to the overall structure, dynamics and stability of the folded protein as well as the role(s) of individual residues in the kinetic pathways between the unfolded and folded states remains less clear. In recent years, there has been a substantial amount of progress in addressing these questions (Alber, 1989; Goldenberg et al., 1989; Lim and Sauer, 1989; Bowie et al., 1990; Dill, 1990; Kim and Baldwin, 1990; Pace et al., 1990; Matthews, 1991). The lysozyme produced by bacteriophage T4 offers an excellent experimental system to address these important questions. In addition, the collaborative research efforts of the Matthews (crystallography, structural bases of protein stability), Schellman (thermodynamics), Hudson (nanosecond dynamics) and our laboratories at the University of Oregon offer a nearly unique environment for the investigation of these issues.

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Authors
  1. D. Eric Anderson
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  2. Jirong Lu
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  3. Lawrence McIntosh
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  4. Frederick W. Dahlquist
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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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Anderson, D.E., Lu, J., McIntosh, L., Dahlquist, F.W. (1993). The Folding, Stability and Dynamics of T4 Lysozyme: A Perspective Using Nuclear Magnetic Resonance. 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_9

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  • DOI: https://doi.org/10.1007/978-1-349-12749-8_9

  • Publisher Name: Palgrave, London

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