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Insights into protein folding from NMR

Academic Article
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Overview

authors

  • Dyson, Jane
  • Wright, Peter

publication date

  • 1996

journal

  • Annual Review of Physical Chemistry  Journal

abstract

  • NMR has emerged as an important tool for studies of protein folding because of the unique structural insights it can provide into many aspects of the folding process. Applications include measurements of kinetic folding events and structural characterization of folding intermediates, partly folded states, and unfolded states. Kinetic information on a time scale of milliseconds or longer can be obtained by real-time NMR experiments and by quench-flow hydrogen-exchange pulse labeling. Although NMR cannot provide direct information on the very rapid processes occurring during the earliest stages of protein folding, studies of isolated peptide fragments provide insights into likely protein folding initiation events. Multidimensional NMR techniques are providing new information on the structure and dynamics of protein folding intermediates and both partly folded and unfolded states.

subject areas

  • Animals
  • Apoproteins
  • Enzymes
  • Kinetics
  • Lactalbumin
  • Magnetic Resonance Spectroscopy
  • Models, Structural
  • Myoglobin
  • Protein Conformation
  • Protein Folding
  • Protein Structure, Secondary
  • Proteins
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Research

keywords

  • NMR hydrogen exchange
  • folding kinetics
  • peptide folding
  • protein folding intermediates
  • unfolded proteins
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Identity

International Standard Serial Number (ISSN)

  • 0066-426X

Digital Object Identifier (DOI)

  • 10.1146/annurev.physchem.47.1.369

PubMed ID

  • 8930101
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Additional Document Info

start page

  • 369

end page

  • 395

volume

  • 47

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