The resurrection of ancient ancestral intrinsically disordered proteins reveals the evolution of a protein-protein interaction in molecular detail.

Orthologous proteins that continuously maintain the same molecular function do not usually diverge beyond a certain level of sequence and structural similarity.

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.

Interactions in protein complexes can be predicted from evolutionary information from genomic sequences.

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.

The emergence of complementary electrostatic potentials after the prokaryotic-to-eukaryotic split drives physical and functional cooperation between canonical class A and class B J-proteins to boost protein disaggregation.

ACCuRET is a flexible new method for measuring the structural dynamics of proteins in solution and membrane proteins in their native environment.

A deep mutational coupling study demonstrates the ability of sequence coevolution methods to reveal the pattern of amino acid interactions underlying protein function.

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.