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

Research output: Contribution to journalArticle

145 Scopus citations

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
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Fingerprint Dive into the research topics of 'Studies by <sup>1</sup>H nuclear magnetic resonance and distance geometry of the solution conformation of the α-amylase inhibitor Tendamistat'. Together they form a unique fingerprint.

  • Cite this