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• W2529452802 startingPage "20160141" @default.
• W2529452802 abstract "Despite the intense efforts of the last decades to understand the thermal stability of proteins, the mechanisms responsible for its modulation still remain debated. In this investigation, we tackle this issue by showing how a multiscale perspective can yield new insights. With the help of temperature-dependent statistical potentials, we analysed some amino acid interactions at the molecular level, which are suggested to be relevant for the enhancement of thermal resistance. We then investigated the thermal stability at the protein level by quantifying its modification upon amino acid substitutions. Finally, a large scale analysis of protein stability—at the structurome level—contributed to the clarification of the relation between stability and natural evolution, thereby showing that the mutational profile of proteins differs according to their thermal properties. Some considerations on how the multiscale approach could help in unravelling the protein stability mechanisms are briefly discussed. This article is part of the themed issue ‘Multiscale modelling at the physics–chemistry–biology interface’." @default.
• W2529452802 created "2016-10-14" @default.
• W2529452802 creator A5073330873 @default.
• W2529452802 creator A5085366265 @default.
• W2529452802 date "2016-11-13" @default.
• W2529452802 modified "2023-10-15" @default.
• W2529452802 title "Improved insights into protein thermal stability: from the molecular to the structurome scale" @default.
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• W2529452802 doi "https://doi.org/10.1098/rsta.2016.0141" @default.
• W2529452802 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5052726" @default.
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