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13 C NMR studies of insulin. Part I—Spectral assignments
Author(s) -
Craik David J.,
Higgins Kerry A.,
Hall Jon G.,
Andrews Peter R.
Publication year - 1989
Publication title -
magnetic resonance in chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.483
H-Index - 72
eISSN - 1097-458X
pISSN - 0749-1581
DOI - 10.1002/mrc.1260270908
Subject(s) - chemistry , dept , carbon 13 nmr , spectral line , pulse sequence , nuclear overhauser effect , two dimensional nuclear magnetic resonance spectroscopy , nmr spectra database , nuclear magnetic resonance spectroscopy , residue (chemistry) , analytical chemistry (journal) , nuclear magnetic resonance , stereochemistry , chromatography , organic chemistry , physics , astronomy
Natural abundance 75 MHz 13 C NMR spectral assignments are reported for bovine and porcine zinc insulin in solution. A large number of protein resonances are well resolved, and approximately 80% of these have been assigned to either residue types or to specific sites within the protein. Assignment techniques included consideration of free amino acid or peptide shifts pH studies and comparison of sequence and spectral differences between bovine and porcine insulin, in addition to the use of NMR relaxation times. The DEPT spectral editing technique was also found to be particularly valuable as an assignment aid. This technique allows subspectra containing only CH, CH 2 or CH 3 carbon types to be generated. The method also produces signal enhancement relative to broad band decoupled 13 C NMR spectra of large proteins which generally have reduced nuclear Overhauser enhancements.