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

Barbara A. Messerle*, Martin Bos, Andreas Schäffer, Milan Vašák, Jeremias H R Kägi, Kurt Wüthrich

*Corresponding author for this work

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

In human metallothionein-2, the exchange rate constants of ten amide protons were found to range from 1.7 × 10-4 to 1 × 10-1 min-1 at pH 6.3 and 8 °C. Most of these slowly exchanging protons could be associated with hydrogen bonds in secondary structure elements of the α-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.

Original languageEnglish
Pages (from-to)781-786
Number of pages6
JournalJournal of molecular biology
Volume214
Issue number3
DOIs
Publication statusPublished - 5 Aug 1990
Externally publishedYes

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