Evidence of oligomerization of bovine insulin in solution given by NMR

Evidence of oligomerization of bovine insulin in solution given by NMR 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png European Biophysics Journal Springer Journals

Evidence of oligomerization of bovine insulin in solution given by NMR

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Publisher
Springer Journals
Copyright
Copyright © 2018 by European Biophysical Societies' Association
Subject
Life Sciences; Biochemistry, general; Biological and Medical Physics, Biophysics; Cell Biology; Neurobiology; Membrane Biology; Nanotechnology
ISSN
0175-7571
eISSN
1432-1017
D.O.I.
10.1007/s00249-018-1310-6
Publisher site
See Article on Publisher Site

Abstract

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.

Journal

European Biophysics JournalSpringer Journals

Published: Jun 1, 2018

References

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