15N Chemical Shifts of Backbone Amides in Bovine Pancreatic Trypsin Inhibitor and Apamin

John Glushka, Maria Lee, Scott Coffin, David Cowburn

Research output: Contribution to journalArticle

87 Scopus citations

Abstract

15N chemical shifts of backbone amides were measured at natural abundance for apamin and bovine pancreatic trypsin inhibitor using heteronuclear multiquantum proton-detected correlated spectroscopy (HMP-COSY). Chemical shift differences from values expected for random-coil peptides were calculated and examined with respect to structural features, including torsion angles and intramolecular hydrogen bonds. A correlation with the torsion angle ψi-1 was observed for the β-sheet residues. No other dominant factor was found to account for the large (up to ±15 ppm) variation from the model peptides. The results suggest that these 15N shifts are sensitive to nonbonded interactions, though there is no systematic variation with respect to a single structural parameter.

Original languageEnglish (US)
Pages (from-to)7716-7722
Number of pages7
JournalJournal of the American Chemical Society
Volume111
Issue number20
DOIs
StatePublished - Sep 1989
Externally publishedYes

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)
  • Biochemistry
  • Colloid and Surface Chemistry

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