Summary
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.
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Laws, D.D., de Dios, A.C. & Oldfield, E. NMR chemical shifts and structure refinement in proteins. J Biomol NMR 3, 607–612 (1993). https://doi.org/10.1007/BF00174614
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DOI: https://doi.org/10.1007/BF00174614