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Structural differences between oxidized and reduced thioredoxin monitored by two-dimensional (1)H NMR spectroscopy

Academic Article
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Overview

authors

  • Dyson, Jane
  • Holmgren, A.
  • Wright, Peter

publication date

  • February 1988

journal

  • FEBS Letters  Journal

abstract

  • Two-dimensional high resolution NMR techniques have been applied to study the structural differences between the oxidized and reduced forms of Escherichia coli thioredoxin in solution. Sequential proton resonance assignments indicate only limited conformational changes; major chemical shift differences are found for a few residues in a beta-strand immediately preceding the active site S-S bridge and the active site itself. Additional resonance shifts are observed for several residues distant in the primary sequence. The X-ray structure of oxidized thioredoxin shows that these residues form a flat hydrophobic surface, close to the active site S-S bridge, which is probably involved in interactions with other protein molecules.

subject areas

  • Amino Acids
  • Bacterial Proteins
  • Escherichia coli
  • Magnetic Resonance Spectroscopy
  • Oxidation-Reduction
  • Protein Conformation
  • Solutions
  • Thioredoxins
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Identity

International Standard Serial Number (ISSN)

  • 0014-5793

Digital Object Identifier (DOI)

  • 10.1016/0014-5793(88)80010-3

PubMed ID

  • 3277863
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Additional Document Info

start page

  • 254

end page

  • 258

volume

  • 228

issue

  • 2

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