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- W2402945017 endingPage "12770" @default.
- W2402945017 startingPage "12760" @default.
- W2402945017 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." @default.
- W2402945017 created "2016-06-24" @default.
- W2402945017 creator A5014097984 @default.
- W2402945017 creator A5036838564 @default.
- W2402945017 creator A5072105936 @default.
- W2402945017 date "2015-09-23" @default.
- W2402945017 modified "2023-09-30" @default.
- W2402945017 title "Stay Wet, Stay Stable? How Internal Water Helps the Stability of Thermophilic Proteins" @default.
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- W2402945017 doi "https://doi.org/10.1021/acs.jpcb.5b05791" @default.
- W2402945017 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5241393" @default.
- W2402945017 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26335353" @default.
- W2402945017 hasPublicationYear "2015" @default.
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