Studies by 1H nuclear magnetic resonance and distance geometry of the solution conformation of the α-amylase inhibitor Tendamistat

Allen D. Kline, Werner Braun, Kurt Wüthrich

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Abstract

This is a preliminary report on the determination of the solution conformation of the α-amylase inhibitor Tendamistat by nuclear magnetic resonance and distance geometry calculations. A characterization is given of the complete polypeptide backbone fold and the side-chains of the presumed active site in this protein. These results are based on complete sequence-specific resonance assignments, a list of 401 distance constraints from nuclear Overhauser effects, 168 distance constraints from hydrogen bonds and disulphide bridges, and 50 torsion angle constraints from measurements of spin-spin coupling constants.

Original languageEnglish (US)
Pages (from-to)377-382
Number of pages6
JournalJournal of Molecular Biology
Volume189
Issue number2
DOIs
StatePublished - May 20 1986

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ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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