The non-covalent assembly of proteins that fold separately is central to many biological
processes, and differs from the permanent macromolecular assembly of protein subunits in …

We compare the geometric and physical–chemical properties of interfaces involved in
specific and non-specific protein–protein interactions in crystal structures reported in the …

Specific protein-protein interactions are essential for cellular functions. Experimentally
determined three-dimensional structures of protein-protein complexes offer the possibility to …

Data sets of 362 structurally nonredundant protein‐protein interfaces and of 57 symmetry‐
related oligomeric interfaces have been used to explore whether the hydrophobic effect that …

The recognition sites in 70 pairwise protein–protein complexes of known three‐dimensional
structure are dissected in a set of surface patches by clustering atoms at the interface. When …

We developed a model of macromolecular interfaces based on the Voronoi diagram and the
related alpha‐complex, and we tested its properties on a set of 96 protein–protein …

Energetic hot spots account for a significant portion of the total binding free energy and
correlate with structurally conserved interface residues. Here, we map experimentally …

Protein–protein interactions play key roles in many cellular processes and their affinities and
specificities are finely tuned to the functions they perform. Here, we present a study on the …

Crystal structures deposited in the Protein Data Bank illustrate the diversity of biological
macromolecular recognition: transient interactions in protein–protein and protein–DNA …

Here, the methods of continuum electrostatics are used to investigate the contribution of
electrostatic interactions to the binding of four protein–protein complexes; barnase–barstar …