Factors enhancing protein thermostability.

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Thermophilic Adaptation of Proteins (2001, methodology): “…dehydrogenases from the hyperthermophile P. furiosus (pfGDH; Tm = 113°C) and from the mesophile Clostridium symbosium (csGDH; Tm = 55°C) were compared (Kumar et al., 2000b). pfGDH and csGDH show an amino acid sequence identity of 34%, and their backbones superimpose with an rms deviation of 1.38 Å.”
Structural genomics of thermotoga maritima proteins shows that contact order is a major determinant of protein thermostability. (2005, methodology): “Several of these studies report more residues in α helices and less residues in loops or disordered regions in proteins from thermophiles (Kumar et al., 2000; Szilagyi and Zavodszky, 2000; Chakravarty and Varadarajan, 2002), but this difference was not the main feature in any of these studies, and…”
Genome-Wide Patterns of Nucleotide Substitution Reveal Stringent Functional Constraints on the Protein Sequences of Thermophiles (2004, background): “Nature 267:for purines in mRNAs, which is also expected to affect 275–276. codon usage (Lao and Forsdyke 2000; Lambros et al. Kollman, J. M., and R. F. Doolittle, 2000 Determination of the relative rates of change for prokaryotic and eukaryotic proteins2003).”