The recent focus on protein-protein interaction networks has increasingly been shifted
towards the disruption of protein complexes, which either are mediated by the binding of a …

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 …

Highlights•Protein–protein interactions are essential for almost all cell processes.•Peptides
are ideal candidates for targeting protein–protein interactions (PPIs).•We survey screening …

Motivation Protein–peptide interactions mediate a wide variety of cellular and biological
functions. Methods for predicting these interactions have garnered a lot of interest over the …

Peptide-protein interactions are ubiquitous in the cell and form an important part of the
interactome. Computational docking methods can complement experimental …

Highlights•We provide an overview of protein-peptide docking methods and their
applications.•Peptide docking tools can be divided on template-based, local and global …

There is a growing interest in the mechanisms and the prediction of how flexible peptides
bind proteins, often in a highly selective and conserved manner. While both existing small …

Protein–protein interactions (PPIs) have emerged as important and challenging targets in
chemical biology and medicinal chemistry. The main difficulty encountered in the discovery …

Protein-peptide interactions are vital for the cell. They mediate, inhibit or serve as structural
components in nearly 40% of all macromolecular interactions, and are often associated with …

In this study, we assess on a large scale the possibility of deriving self‐inhibitory peptides
from protein domains with globular architectures. Such inhibitory peptides would inhibit …