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

While there are a number of structurally non-redundant datasets of protein monomers, there
is none of protein-protein interfaces. Yet, the availability of such a dataset is expected to …

The number of protein-peptide interactions in a cell is so large that experimental
determination of all these complex structures would be a daunting task. Although homology …

Peptide-protein interactions are very prevalent, mediating key processes such as signal
transduction and protein trafficking. How can peptides overcome the entropic cost involved …

At the heart of protein–protein interactions are protein–protein interfaces where the direct
physical interactions occur. By developing and applying an efficient structural alignment …

The general similarity in the forces governing protein folding and protein-protein
associations has led us to examine the similarity in the architectural motifs between the …

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

Abstract PixelDB, the Peptide Exosite Location Database, compiles 1966 non‐redundant,
high‐resolution structures of protein–peptide complexes filtered to minimize the impact of …

Many important protein–protein interactions are mediated by the binding of a short peptide
stretch in one protein to a large globular segment in another. Recent efforts have provided …

Proteins fold into a well‐defined structure as a result of the collapse of the polypeptide chain,
while transient protein‐complex formation mainly is a result of binding of two folded …