Structure of cubic insulin crystals in glucose solutions

Biophysical Journal
B Yu, D L Caspar

Abstract

X-ray structures of cubic insulin crystals in high concentrations of glucose at different pH levels and temperatures have been refined to high resolution. We have identified one glucose-binding site near the N-terminus of the A-chain whose occupancy is pH dependent. The effects of reduced water activity on the ordered protein and solvent structures have been examined. Our analysis showed no notable conformational changes in the ordered protein structures or ordered solvent molecules near the protein surface, but the presence of glucose does have a significant effect on the overall density distribution of the bulk solvent in the solvent-accessible volume. We compared the structure of cubic insulin at room temperature and liquid-nitrogen temperature, under identical solvent conditions, using glucose as a cryoprotectant. In this case, we found that the average temperature factor of the protein is reduced and more water molecules can be identified, but there are no significant changes in the protein conformation.

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Citations

Sep 24, 2004·Journal of Molecular Recognition : JMR·Robert S Root-Bernstein
Oct 9, 2001·International Journal of Biological Macromolecules·M FalconiM T Cambria
Mar 9, 2010·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·V I TimofeevI P Kuranova
Apr 17, 2012·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Anja BurkhardtAlke Meents
Jun 26, 2009·Cellular and Molecular Life Sciences : CMLS·Robert Root-Bernstein, Jessica Vonck
Mar 21, 2006·BioEssays : News and Reviews in Molecular, Cellular and Developmental Biology·Axel HundingRobert Root-Bernstein
Aug 26, 2017·Journal of Structural Biology·Alexei S Soares, Donald L D Caspar
Jun 28, 2000·Analytical Biochemistry·S DespaM Ameloot

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