Protein–protein interactions form central elements of almost all cellular processes.
Knowledge of the structure of protein–protein complexes but also of the binding affinity is of …

A systematic study of the linear interaction energy (LIE) method and the possible
dependence of its parameterization on the force field and system (receptor binding site) is …

Highlights•Reviewed scoring schemes and conformational sampling for protein–protein
complex structure prediction.•Discussed the database for binding affinity of complexes and …

Recent advances in high-throughput experimental methods for the identification of protein
interactions have resulted in a large amount of diverse data that are somewhat incomplete …

Many essential cellular processes such as signal transduction, transport, cellular motion and
most regulatory mechanisms are mediated by protein–protein interactions. In recent years …

Gaining insights into the structural determinants of protein–protein interactions holds the key
for a deeper understanding of biological functions, diseases and development of …

We present an energy function for predicting binding free energies of protein–protein
complexes, using the three‐dimensional structures of the complex and unbound proteins as …

Ligand binding affinity prediction is one of the most important applications of computational
chemistry. However, accurately ranking compounds with respect to their estimated binding …

The accurate prediction of protein–protein complex geometries is of major importance to
ultimately model the complete interactome of interacting proteins in a cell. A major …

We have assembled a nonredundant set of 144 protein–protein complexes that have high‐
resolution structures available for both the complexes and their unbound components, and …