Conformations of side chains of somatostatin very high field proton NMR studies

David H. Live, Donald G. Davis, William C. Agosta, David Cowburn

Research output: Contribution to journalReview article

5 Scopus citations

Abstract

The high field proton NMR spectra (500 and 600 MHz) of the peptide hormone somatostatin in D2O are reported. The results obtained are used to derive values of the couplings and chemical shifts related to the solution conformation of several of the side chains. This work resolves a discrepancy in the literature concerning the assignments of resonances in the spectrum. It also provides a means of testing the accuracy of obtaining values for these couplings and shifts in previous 2D NMR studies at lower field from strongly coupled multiplets in spectra of this complexity.

Original languageEnglish (US)
Pages (from-to)211-215
Number of pages5
JournalMagnetic Resonance in Chemistry
Volume19
Issue number4
DOIs
StatePublished - 1982
Externally publishedYes

ASJC Scopus subject areas

  • Chemistry(all)
  • Materials Science(all)

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