Explanation of the stability of thermophilic proteins based on unique micromorphology

Biophysical Journal
Simone MelchionnaGiuseppe Briganti

Abstract

Two mesophilic/thermophilic variants of the G-domain of the elongation factor Tu were studied via molecular dynamics simulations. By analyzing the simulation data via the Voronoi space tessellation, we have found that the two proteins have the same macromolecular packing, while the water-exposed surface area is larger for the thermophile. A larger coordination with water is probably due to a peculiar corrugation of the exposed surface of this species. From an enthalpic point of view, the thermophile shows a larger number of intramolecular hydrogen bonds, stronger electrostatic interactions, and a flatter free-energy landscape. Overall, the data suggest that the specific hydration state enhances macromolecular fluctuations but, at the same time, increases thermal stability.

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Citations

Apr 8, 2011·Protein Engineering, Design & Selection : PEDS·Ronny MartinezDanilo Roccatano
Jul 18, 2014·PLoS Computational Biology·Fabrizio Pucci, Marianne Rooman
Apr 29, 2009·International Journal of Molecular Sciences·Atsushi Mukaiyama, Kazufumi Takano
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Sep 4, 2015·The Journal of Physical Chemistry. B·Debashree ChakrabortyFabio Sterpone
Oct 6, 2009·Biochimica Et Biophysica Acta·Hana SanderováLibor Krásný
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Mar 15, 2011·Journal of Physics. Condensed Matter : an Institute of Physics Journal·Fabio SterponeSimone Melchionna
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Dec 17, 2008·The Journal of Physical Chemistry. B·Fabio SterponeSimone Melchionna
Oct 16, 2014·The Journal of Physical Chemistry. B·Obaidur RahamanFabio Sterpone
Mar 13, 2012·Journal of Chemical Theory and Computation·Enrique MarcosRamon Crehuet

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