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13C NMR studies of insulin. Part I—Spectral assignments

✍ Scribed by David J. Craik; Kerry A. Higgins; Jon G. Hall; Peter R. Andrews

Publisher
John Wiley and Sons
Year
1989
Tongue
English
Weight
918 KB
Volume
27
Category
Article
ISSN
0749-1581

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✦ Synopsis

Natural abundance 75 MHz I3C 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, or CH, carbon types to be generated. The method also produces signal enhancement relative to broad band decoupled I3C NMR spectra of large proteins which generally have reduced nuclear Overhauser enhancements.

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