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.

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

Integrating multiple protein language models using protein geometric graphs can dramatically improve the model performance for predicting the contacting residue pairs between interacting proteins.

The utilization of hydrogen/deuterium exchange mass spectrometry reveals dynamic insights and interactions driving liquid-liquid demixing of the chromosome passenger complex.

The N-terminal domain of Staphylococcus aureus GpsB, a scaffolding protein, forms an atypical asymmetric dimer and binds to the C-termini of FtsZ and PBP4, influencing the localization and regulation of both the Z-ring and cell wall synthesis.

AlphaFold-Multimer was used to investigate extracellular protein interactions involved in mammalian egg-sperm recognition, suggesting a putative pentameric complex that includes TMEM81, a sperm protein not previously involved in gamete recognition.

A new machine-learning toolbox unveils coevolutionary protein motifs related to structure, function, and phylogeny from sequence information only.

The dynamic structure of respiratory complex I from mesophilic bacterium is revealed and demonstrates existence of uncoupled conformations in the bacterial complex.

The first atomic resolution structure of a mitochondrial respiratory complex from plants provides insight into the assembly and evolution of respiration in autotrophic eukaryotes.

The AlphaFold protein structure prediction network can be specialized for T cell receptor docking, leading to improved models of ternary complexes and some ability to discriminate correct from incorrect peptide epitopes.