A generalizable approach to understanding the logic of molecular recognition reveals the contributions of individual residues to the specificity of protein-protein interactions.

The helical cell shape of Helicobacter pylori depends on the polymerizing cytoskeletal protein CcmA’s recruitment to the cell envelope by Csd5 and CcmA’s indirect stabilization of a periplasmic cell wall hydrolase via interactions with the transmembrane protein Csd7.

Biased research interest in proteins and aggregation of interactions from multiple studies can explain why node degree distributions in protein-protein interaction networks follow a power law.

An enrichable cross-linker with optional isotope labeling quadruples the number of cross-linked peptides identified from high-complexity samples, enhancing proteome-wide analysis of protein-protein interactions and protein conformational changes by mass spectrometry.

In rotaviruses, the selective packaging of eleven distinct genomic RNA segments requires virus-encoded protein NSP2 to alter the RNA structures, facilitating their interactions with each other.

Forcing protein associations across the proteome reveals the cell's tolerance for diverse protein interactions and reveals the interactions that affect growth.

Affinity capture of polyribosomes followed by RNAseq(ACAPSeq) is a technique that harnesses massively parallel sequencing to identify protein-protein interactions from any source from which polyribosomes can be purified.

The number of contacts at the interface of a protein–protein complex, together with the properties of the surface, provides a simple, but well-performing predictor of binding affinity.

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

A post-translational modification called O-GlcNAcylation modulates the activity of the SOX2 transcription factor in pluripotent stem cells.