NMR chemical shifts and structure refinement in proteins

David D. Laws, Angel C. de Dios, Eric Oldfield

Research output: Contribution to journalArticlepeer-review


Computation of the 13Cα chemical shifts (or shieldings) of glycine, alanine and valine residues in bovine and Drosophila calmodulins and Staphylococcal nuclease, and comparison with experimental values, is reported using a gauge-including atomic orbital quantum-chemical approach. The full ≈24 ppm shielding range is reproduced (overall r.m.s.d.=1.4 ppm) using 'optimized' protein structures, corrected for bond-length/bond-angle errors, and rovibrational effects.

Original languageEnglish (US)
Pages (from-to)607-612
Number of pages6
JournalJournal of Biomolecular NMR
Issue number5
StatePublished - Sep 1993


  • Ab initio
  • Calmodulin
  • Chemical shift
  • Staphylococcal nuclease

ASJC Scopus subject areas

  • Biochemistry
  • Spectroscopy


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