Stay Wet, Stay Stable? How Internal Water Helps the Stability of Thermophilic Proteins

The Journal of Physical Chemistry. B
Debashree ChakrabortyFabio Sterpone

Abstract

We present a systematic computational investigation of the internal hydration of a set of homologous proteins of different stability content and molecular complexities. The goal of the study is to verify whether structural water can be part of the molecular mechanisms ensuring enhanced stability in thermophilic enzymes. Our free-energy calculations show that internal hydration in the thermophilic variants is generally more favorable, and that the cumulated effect of wetting multiple sites results in a meaningful contribution to stability. Moreover, thanks to a more effective capability to retain internal water, some thermophilic proteins benefit by a systematic gain from internal wetting up to their optimal working temperature. Our work supports the idea that internal wetting can be viewed as an alternative molecular variable to be tuned for increasing protein stability.

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Citations

Feb 26, 2016·The Journal of Physical Chemistry. B·Marina KatavaFabio Sterpone
May 18, 2016·Chemical Reviews·Marie-Claire Bellissent-FunelAngel E Garcia
Mar 11, 2017·The Journal of Physical Chemistry. B·Gregory S CusterSilvina Matysiak
Jun 10, 2018·The Journal of Chemical Physics·Filip PerssonBertil Halle
Jan 16, 2021·Molecular Biology and Evolution·Michel LecocqCéline Brochier-Armanet
Jul 12, 2017·The Journal of Physical Chemistry. B·Xiaomin JingEngin H Serpersu

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