C-13 NMR spectral studies of the thyroid hormone transport protein, transthyretin and the pancreatic insulin storage moiety, the zinc-insulin hexamer.
The DEPT spectral editing technique was used to separate the CH, CH2 and CH3 resonances in the C-13 NMR spectra of transthyretin and the porcine zinc insulin hexamer. The advantages of this technique in terms of spectral simplification and sensitivity enhancement for 13C NMR of proteins is discussed. Spin-lattice relaxation time and nuclear Overhauser effect measurements of the backbone C-alpha and aliphatic sidechain carbons provided information about the dynamics of the proteins in solution and the relative mobility of some sidechain groups.
D000818:Animals; D002247:Carbon Isotopes; D006801:Humans; D007328:Insulin; D009682:Magnetic Resonance Spectroscopy / Q000379:methods; D008970:Molecular Weight; D010179:Pancreas / Q000378:metabolism*; D011228:Prealbumin; D011487:Protein Conformation; D013552:Swine; D015032:Zinc
D002247:Carbon Isotopes; D007328:Insulin; D011228:Prealbumin; D015032:Zinc