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Folding of a beta-sheet protein monitored by real-time NMR spectroscopy

Academic Article
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Overview

authors

  • Mizuguchi, M.
  • Kroon, G. J.
  • Wright, Peter
  • Dyson, Jane

publication date

  • May 2003

journal

  • Journal of Molecular Biology  Journal

abstract

  • At low ionic strength, apoplastocyanin forms an unfolded state under non-denaturing conditions. The refolding of this state is sufficiently slow to allow real-time NMR experiments to be performed. Folding of apoplastocyanin, initiated by the addition of salt and followed by real-time 2D 1H-15N heteronuclear single quantum coherence (HSQC) spectroscopy, is highly cooperative. A concomitant increase in the intensity of both sequential and long-range nuclear Overhauser effects (NOEs) between backbone amide protons in successive acquisitions of 1H-15N HSQC-NOESY-HSQC spectra provides the first direct observation of the development of structure-specific NOEs as a protein folds. Our results show that the local and long-range interactions in the native apoplastocyanin are formed simultaneously, consistent with highly cooperative formation of the native structure.

subject areas

  • Apoproteins
  • In Vitro Techniques
  • Kinetics
  • Models, Molecular
  • Nuclear Magnetic Resonance, Biomolecular
  • Plastocyanin
  • Protein Folding
  • Protein Structure, Secondary
  • Recombinant Proteins
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Research

keywords

  • beta-sheet folding
  • plastocyanin
  • proline isomerism
  • slow protein folding
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Identity

International Standard Serial Number (ISSN)

  • 0022-2836

Digital Object Identifier (DOI)

  • 10.1016/s0022-2836(03)00349-8

PubMed ID

  • 12729749
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Additional Document Info

start page

  • 1161

end page

  • 1171

volume

  • 328

issue

  • 5

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