A few months ago we published an explorative work focusing on the possible contribution of water molecules buried in the interior of proteins to their different thermal stabilities [see here for the paper]. The study-case was a pair of homologous GTPase domains from a mesophilic and a hyperthermophilic organism, respectively. Now, we extended our approach by considering a large set of homologous pairs. Let's list the main findings. Firstly, for some homologues internal water gives a meaningful contribution to the stability gap in favour of the thermophilic variant. This was probed at ambient condition. Secondly, when considering the behaviour at high temperature, we found that thermophilic proteins are more keen to maintain their internal cavities wet, and therefore benefiting by this wetting. We propose that internal hydration can be viewed as an alternative tuneable variable for the engineering of proteins with enhanced stability. Enjoy the manuscript here.
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