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Mapping long-range contacts in a highly unfolded protein

Academic Article
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Overview

authors

  • Lietzow, M. A.
  • Jamin, M.
  • Dyson, Jane
  • Wright, Peter

publication date

  • September 2002

journal

  • Journal of Molecular Biology  Journal

abstract

  • Insights into the earliest events in protein folding can be obtained by analysis of the conformational propensities of unfolded or partly folded states. The structure of the acid-unfolded state of apomyoglobin has been characterized using paramagnetic spin labeling and NMR. Nitroxide side-chains, introduced by coupling to mutant cysteine residues at positions 18, 77, and 133, were used as probes of chain compaction and long-range tertiary contacts. Significant interactions are observed within and between the N and C termini, while the central region of the polypeptide chain behaves as a random polymer. Even in this highly denatured form, the protein samples transient compact states in which there are native-like contacts between the N and C-terminal regions.

subject areas

  • Apoproteins
  • Mutagenesis
  • Myoglobin
  • Protein Folding
  • Protein Structure, Tertiary
  • Spin Labels
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Research

keywords

  • apomyoglobin
  • protein folding
  • spin label
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Identity

International Standard Serial Number (ISSN)

  • 0022-2836

Digital Object Identifier (DOI)

  • 10.1016/s.0022-2836(02)00847-1

PubMed ID

  • 12270702
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Additional Document Info

start page

  • 655

end page

  • 662

volume

  • 322

issue

  • 4

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