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

144 Citations (Scopus)

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

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Amylases
Disulfides
Hydrogen
Catalytic Domain
Magnetic Resonance Spectroscopy
Peptides
Proteins
tendamistate

ASJC Scopus subject areas

  • Virology

Cite this

Studies by 1H nuclear magnetic resonance and distance geometry of the solution conformation of the α-amylase inhibitor Tendamistat. / Kline, Allen D.; Braun, Werner; Wüthrich, Kurt.

In: Journal of Molecular Biology, Vol. 189, No. 2, 20.05.1986, p. 377-382.

Research output: Contribution to journalArticle

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