A number of studies have addressed the question of which are the critical residues at protein‐
binding sites. These studies examined either a single or a few protein–protein interfaces …

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 …

Proteins are capable of highly specific interactions and are responsible for a wide range of
functions, making them attractive in the pursuit of new therapeutic options. Previous studies …

We compared the modes of interaction between protein-peptide interfaces and those
observed within monomeric proteins and found surprisingly few differences. Over 65% of …

We analyze the characteristics of protein–protein interfaces using the largest datasets
available from the Protein Data Bank (PDB). We start with a comparison of interfaces with …

Reliably pinpointing which specific amino acid residues form the interface (s) between a
protein and its binding partner (s) is critical for understanding the structural and …

We present an analysis of the water molecules immobilized at the protein–protein interfaces
of 115 homodimeric proteins and 46 protein–protein complexes, and compare them with …

A rapid increase in the number of experimentally derived three‐dimensional structures
provides an opportunity to better understand and subsequently predict protein–protein …

Protein recognition is one of the most challenging and intriguing problems in structural
biology. Despite all the available structural, sequence and biophysical information about …

We used a nonredundant set of 621 protein–protein interfaces of known high‐resolution
structure to derive residue composition and residue–residue contact preferences. The …