NMR chemical shifts and structure refinement in proteins.
 

NMR chemical shifts and structure refinement in proteins.

Related Articles NMR chemical shifts and structure refinement in proteins.

J Biomol NMR. 1993 Sep;3(5):607-12

Authors: Laws DD, de Dios AC, Oldfield E

Computation of the 13C alpha 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 approximately 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.

PMID: 8219743 [PubMed - indexed for MEDLINE]



Source: PubMed