The protein hormone insulin exists in several forms in nature, and a large number of modified sequences are used in phar - macy. They differ by physicochemical properties and efficiency of biological action. Pancreatic bovine insulin was studied 1 13 in an acidic solution by nuclear magnetic resonance spectroscopy. H and C NMR signal assignment of backbone and side chains was made by analysis of a set of 2D spectra obtained on a sample with natural isotope abundance. The presence of certain secondary structure elements was revealed on a qualitative level based on nuclear Overhauser effect spectroscopy, which are similar to those observed in the crystal structure. The C-terminus of the B-chain possessed a remarkable flex - ibility. The molecule was shown to exist in exchange with oligomers based on its self-diffusion coefficient and correlation time measurements performed at different concentrations. Certain signals in the NOESY and HSQC spectra are consistent with the presence of minor conformers; this is an obstacle in simulating the molecular structure under the conditions used in the experiment. Keywords Bovine insulin · Secondary structure · NMR · NOESY · DOSY · Oligomerization Introduction life. Some types of the disease, especially type 2, are treated by sulfonylurea; sometimes pramlintide (Ryan et al.
European Biophysics Journal – Springer Journals
Published: Jun 1, 2018
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