Chemical Shifts in Proteins: An Ab Initio Study of Carbon-13 Nuclear Magnetic Resonance Chemical Shielding in Glycine, Alanine, and Valine Residues

Angel C. de Dios, John G. Pearson, Eric Oldfield

Research output: Contribution to journalArticlepeer-review

Abstract

Using gauge-including atomic orbital self-consistent field ab initio quantum chemical methods, we have computed the effects of bond lengths, bond angles, and torsion angles on the carbon-13 chemical shielding of Cα (and Cβ) sites in model fragments for glycine, alanine, and valine residues in proteins. Predicted chemical shieldings are highly sensitive to bond length variations, and we show that it is essential to relax or energy minimize protein structures (to remove large errors associated with bond length uncertainties) in order to successfully predict experimental 13C NMR spectra.

Original languageEnglish (US)
Pages (from-to)9768-9773
Number of pages6
JournalJournal of the American Chemical Society
Volume115
Issue number21
DOIs
StatePublished - Oct 1 1993

ASJC Scopus subject areas

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

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