Evidence of oligomerization of bovine insulin in solution given by NMR
Autor: | S. V. Efimov, Yu.O. Zgadzay, N. B. Tarasova, Vladimir V. Klochkov |
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Rok vydání: | 2018 |
Předmět: |
0301 basic medicine
Biophysics Nuclear Overhauser effect 010402 general chemistry 01 natural sciences 03 medical and health sciences Animals Insulin Molecule Amino Acid Sequence Protein Structure Quaternary Nuclear Magnetic Resonance Biomolecular Protein secondary structure Conformational isomerism Chemistry General Medicine Nuclear magnetic resonance spectroscopy Carbon-13 NMR 0104 chemical sciences Solutions Crystallography 030104 developmental biology Cattle Protein Multimerization Two-dimensional nuclear magnetic resonance spectroscopy Heteronuclear single quantum coherence spectroscopy |
Zdroj: | European Biophysics Journal. 47:881-889 |
ISSN: | 1432-1017 0175-7571 |
Popis: | The protein hormone insulin exists in several forms in nature, and a large number of modified sequences are used in pharmacy. They differ by physicochemical properties and efficiency of biological action. Pancreatic bovine insulin was studied in an acidic solution by nuclear magnetic resonance spectroscopy. [Formula: see text]H and [Formula: see text]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 flexibility. 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. |
Databáze: | OpenAIRE |
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