Thermophilic Adaptation of Proteins

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Amino acid composition of proteins reduces deleterious impact of mutations (2013, methodology): “(8) for the 8 3 8 interaction matrix of the subgroup and their normalized natural occurrence frequencies.”
The thermal limits to life on Earth (2014, background): “In these, structural integrity is associated with the presence of large molecular chaperones and a range of small compatible solutes (Sterner & Liebl 2001).”
Avoiding Dangerous Missense: Thermophiles Display Especially Low Mutation Rates (2009, background): “If the Kimura conjecture is correct, then increasing the average deleterious impact of a spontaneous mutation (and thus converting many neutral or nearly-neutral mutations to deleterious mutations) would lower the rate of mutation, at least on an evolutionary time scale. The concept of an equilibriu”
The Biocatalytic Potential of Extremophiles and Extremozymes (2004, background): “Several three-dimensional structures have been resolved and compared with those of mesophilic counterparts, with the ultimate goal of elucidating the mechanisms underlying thermostability (37,38).”
Structural genomics of thermotoga maritima proteins shows that contact order is a major determinant of protein thermostability. (2005, background): “Whereas most organisms do not survive at temperatures above 50°C, a small number of hyperthermophilic bacteria and archea thrive at temperatures over 80°C and in some cases greater than 110°C (Sterner and Liebl, 2001).”