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- W2162782223 endingPage "332" @default.
- W2162782223 startingPage "323" @default.
- W2162782223 abstract "This article shows that the stability profiles of thermophilic proteins are significantly displaced toward higher temperatures as compared to those of mesophilic proteins. A similar trend characterizes the aqueous transfer of N-alkyl amides. In fact, as a general feature of transfer processes, liquid dissolution profiles are centered at temperatures higher than those of solid ones. This behavior is governed by packing contributions. A partition of the unfolding thermodynamics based on the analysis of phenomenological temperatures common to dissolution and unfolding phenomena provides a clue to understanding the mechanism of thermal stabilization. In fact, the position of stability profiles along the temperature axis does not appear to depend on solvation of internal residues. Instead, it is notably affected by solidlike components, whose progressive decrease appears to drive the heat denaturation temperature increase of most thermostable proteins. As a corollary, it is shown that there are actually two limiting mechanisms of thermal stabilization." @default.
- W2162782223 created "2016-06-24" @default.
- W2162782223 creator A5086934848 @default.
- W2162782223 date "2003-11-24" @default.
- W2162782223 modified "2023-10-15" @default.
- W2162782223 title "Phenomenological similarities between protein denaturation and small-molecule dissolution: Insights into the mechanism driving the thermal resistance of globular proteins" @default.
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- W2162782223 doi "https://doi.org/10.1002/prot.10574" @default.
- W2162782223 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/14696194" @default.
- W2162782223 hasPublicationYear "2003" @default.
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