Abstract
Bacteria growing at high temperatures have a high proportion of charged residues in their proteins to stabilize their 3D structure. By mining 175 disparate bacterial and archaeal proteomes we discovered that, against the general trend for charged residues, the frequency of aspartic acid residues decreases strongly as natural growth temperature increases. We conclude that organisms likely adapt to high temperatures by minimizing the harmful consequences of spontaneous chemical transformations of Asp residues.