Principles of protein stability derived from protein engineering experiments

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De novo protein design, a retrospective (2020, background): “It became generally accepted that the packing of hydrophobic residues in the solvent-accessible interiors of proteins contributed significantly to the driving force for water-soluble protein folding, and that polar interactions, although less favorable, often helped define the detailed geometries of”
Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: results of a comprehensive survey. (2000, background): “On the contrary, most of them do have such contributions, as is revealed by site-directed mutagenesis experiments (see [47] for a review).”
From DNA sequence to improved functionality: using protein sequence comparisons to rapidly design a thermostable consensus phytase. (2000, background): “Despite extensive knowledge of the general mechanisms governing protein stability (Dill et al., 1989; Dill, 1990; Fersht and Serrano, 1993; Matthews, 1993; Cordes et al., 1996) no rapid and reliable procedures are available for increasing the thermostability of a given protein.”
Directed evolution converts subtilisin E into a functional equivalent of thermitase. (1999, background): “A more promising approach to elucidating molecular mechanisms of thermostabilization is to study engineered proteins in which the effects of specific amino acid substitutions can be pinpointed (Fersht and Serrano, 1993; Matthews, 1995).”