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Proton NMR Studies of Protein Dynamics and Folding: Applications of Magnetization Transfer NMR

  • Christopher M. Dobson
  • Philip A. Evans

Abstract

When a protein exists at equilibrium in more than one conformational state it may be possible to observe separately in the NMR spectrum resonances corresponding to the different states. Provided that interconversion between these states occurs at suitable rates, magnetization transfer techniques may be used to detect it, and in favorable cases to obtain rate constants for specific conformational transitions. Results of one- and two-dimensional 1H NMR experiments with lysozyme and staphylococcal nuclease are used to illustrate the potentials of such an approach to studying the dynamics and folding of proteins.

Keywords

Magnetization Transfer Folding Pathway Staphylococcal Nuclease Minor Resonance Obtain Rate Constant 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Plenum Press, New York 1986

Authors and Affiliations

  • Christopher M. Dobson
    • 1
  • Philip A. Evans
    • 1
  1. 1.Inorganic Chemistry LaboratoryUniversity of OxfordOxfordUK

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