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Amide proton-exchange in human metallothionein-2 measured by nuclear-magnetic-resonance spectroscopy

Academic Article
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Overview

authors

  • Messerle, B. A.
  • Bos, M.
  • Schaffer, A.
  • Vasak, M.
  • Kagi, J. H. R.
  • Wuthrich, Kurt

publication date

  • 1990

journal

  • Journal of Molecular Biology  Journal

abstract

  • In human metallothionein-2, the exchange rate constants of ten amide protons were found to range from 1.7 x 10(-4) to 1 x 10(-1) min-1 at pH 6.3 and 8 degrees C. Most of these slowly exchanging protons could be associated with hydrogen bonds in secondary structure elements of the alpha-domain. Amide proton exchange rates thus present an additional criterion for the structural characterization of different metallothioneins, which could be particularly valuable for comparisons of different homologous protein preparations containing nuclear magnetic resonance-inactive metal ions, where the metal-polypeptide co-ordinative bonds cannot be identified directly.

subject areas

  • Amides
  • Amino Acid Sequence
  • Humans
  • Hydrogen Bonding
  • Magnetic Resonance Spectroscopy
  • Metallothionein
  • Molecular Sequence Data
  • Protein Conformation
  • Protons
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Identity

International Standard Serial Number (ISSN)

  • 0022-2836

Digital Object Identifier (DOI)

  • 10.1016/0022-2836(90)90292-t

PubMed ID

  • 2167380
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Additional Document Info

start page

  • 781

end page

  • 786

volume

  • 214

issue

  • 3

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