We explore the fundamental principles of protein evolution. We unravel, at atomic detail, features of proteins that promote the rapid acquisition of new functions such as conformational diversity (one sequence adopting multiple structures), promiscuity (latent, coincidental functions), structural stability, and the potential of neutral mutations to promote adaptation. Our reconstructions of the ancestors and intermediates that led of today’s proteins are providing crucial insights as to how evolution shapes protein properties such as stability and folding, or enzyme catalytic efficiency and specificity.
A "lab review" by Tyler Hampton.