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.
Building on previous work (Skene et al., 2014), we show that a new ChIP-seq protocol provides superior resolution and ease of use at low sequence depth of coverage for generating genome-wide maps of protein binding.
Experimentally reconstructing the evolution of the molecular complex that animals use to orient the mitotic spindle establishes a simple genetic and physical mechanism for the emergence of a function essential for multicellularity.
New hybrid structure determination methods leveraging the inherent biophysical properties of a macromolecule through molecular dynamics simulations provide accurate and cost-efficient ways of achieving atomic structures from high resolution cryo-electron density maps.
In the ancestor of mammals, a multifunctional innate immune protein evolved when a mutation enhanced the protein’s pro-inflammatory activity and proteolytic regulation without disrupting the protein’s antimicrobial activity.