Solvent accessibility and purifying selection within proteins of Escherichia coli and Salmonella enterica.

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Structural determinants of protein evolution are context-sensitive at the residue level. (2009, background): “…early in the history of structural biology (Perutz et al. 1965) and has been repeatly confirmed since (Overington et al. 1992; Goldman et al. 1998; Bustamante et al. 2000; Choi et al. 2006; Conant and Stadler 2009) that residues buried in a protein’s core are more likely to remain conserved…”
The inherent mutational tolerance and antigenic evolvability of influenza hemagglutinin (2014, background): “A confounding factor in comparing mutational tolerance across different sets of residues is that sites with higher solvent accessibility are typically more tolerant of mutations (Bustamante et al., 2000; Ramsey et al., 2011).”
The amino-acid mutational spectrum of human genetic disease (2003, background): “[21]), who suggested that the dominant mechanism by which disease mutations damage protein function is a decrease in protein stability, as opposed to mutations of active-site residues (usually located on the protein surface).”