A new method of protein structure prediction that incorporates residue–residue co-evolution information into the Rosetta structure prediction program was used to develop models for 58 large protein families that had no previous structural information.
Statistics on the frequencies of pi interactions in folded protein structures enable successful prediction of intrinsically disordered protein phase separation, with clear implications for a physical understanding of cellular organization.
Co-evolving residue pairs in the different components of a protein complex almost always make contact across the protein–protein interface, thus providing powerful restraints for the modeling of protein complexes.
Discovery of the structural basis for recognition and uptake of a human precursor for body odour production reveals an important role for bacterial peptide transport and novel routes to prevent its production in humans.
A computational method identifies the functions of orphan enzymes by organizing them into metabolic pathways; the prediction of a new l-gulonate catabolic pathway is experimentally tested and confirmed.