Replicating experimental evolution from ancestral proteins shows that historical contingency steadily overwhelms chance and necessity as the primary cause of evolutionary variation in molecular sequences on long phylogenetic timescales.
Reconstructing ancestral enzymes has revealed that a switch in kinase substrate preference evolved via an expanded specificity intermediate that is tolerated in vivo, thus providing a path for kinase diversification.
A gain-of-function in a new chemical defense resulted in no trade-offs and and independent evolution between novel and ancestral defenses, suggesting low redundancy among different defensive chemicals.
Admixture-mediated adaptation to malaria in a human population demonstrates that detectible signatures in genomic patterns of ancestry can be leveraged to better characterize recent selection in populations with mixed ancestry.
Sponges and ctenophores lack hypoxia-inducible factors, suggesting that the metazoan last common ancestor could have lived aerobically under severe hypoxia and did not need to regulate its transcription in response to oxygen availability.
Reengineering the nucleotide-binding pocket of an extant ATPase to restore ancestral GTPase activity revealed an ATP-dependent intermediate required for function and suggested why the protein evolved to use ATP.