Polypeptide fold in the two metal clusters of metallothionein-2 by nuclear magnetic resonance in solution

Werner Braun, Gerhard Wagner, Erich Wörgötter, Milan Vašák, Jeremias H R Kägi, Kurt Wüthrich

Research output: Contribution to journalArticle

120 Citations (Scopus)

Abstract

The solution conformation of rabbit liver Cd7 2+-metallothionein-2 was determined by nuclear magnetic resonance (n.m.r.) and distance geometry. The n.m.r. data are based on complete sequence-specific resonance assignments for the polypeptide chain. This letter describes the global arrangement of the polypeptide chain, which forms two distinct domains containing metal clusters of three and four Cd ions, respectively.

Original languageEnglish (US)
Pages (from-to)125-129
Number of pages5
JournalJournal of Molecular Biology
Volume187
Issue number1
DOIs
StatePublished - Jan 5 1986
Externally publishedYes

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Metallothionein
Magnetic Resonance Spectroscopy
Metals
Peptides
Ions
Rabbits
Liver

ASJC Scopus subject areas

  • Virology

Cite this

Polypeptide fold in the two metal clusters of metallothionein-2 by nuclear magnetic resonance in solution. / Braun, Werner; Wagner, Gerhard; Wörgötter, Erich; Vašák, Milan; Kägi, Jeremias H R; Wüthrich, Kurt.

In: Journal of Molecular Biology, Vol. 187, No. 1, 05.01.1986, p. 125-129.

Research output: Contribution to journalArticle

Braun, Werner ; Wagner, Gerhard ; Wörgötter, Erich ; Vašák, Milan ; Kägi, Jeremias H R ; Wüthrich, Kurt. / Polypeptide fold in the two metal clusters of metallothionein-2 by nuclear magnetic resonance in solution. In: Journal of Molecular Biology. 1986 ; Vol. 187, No. 1. pp. 125-129.
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