Proline residues have unique roles in protein folding, structure, and function. Proline and the
aromatic amino acids comprise the encoded cyclic protein residues. Aromatic protein side …

An increasing number of SH3 domain–ligand interactions continue to be described that
involve the conserved peptide-binding surface of SH3, but structurally deviate substantially …

Introduction to Proteins provides a comprehensive and state-of-the-art introduction to the
structure, function, and motion of proteins for students, faculty, and researchers at all levels …

Protein–protein interactions occurring via the recognition of short peptide sequences by
modular interaction domains play a central role in the assembly of signalling protein …

The empirical force field Fold-X was developed previously to allow rapid free energy
calculations in proteins. Here, we present an enhanced version of the force field allowing …

In mammalian cells, much of signal transduction is mediated by weak protein–protein
interactions between globular peptide-binding domains (PBDs) and unstructured peptidic …

Intrinsically disordered proteins (IDPs) carry out many biological functions. They lack a
stable three-dimensional structure, but rather adopt many different conformations in dynamic …

The advent of advanced molecular modeling software, big data analytics, and high-speed
processing units has led to the exponential evolution of modern drug discovery and better …

The formation of specific protein interactions plays a crucial role in most, if not all, biological
processes, including signal transduction, cell regulation, the immune response and others …

The transcriptional corepressors BCOR, SMRT, and NCoR are known to bind competitively
to the BCL6 BTB domain despite the fact that BCOR has no detectable sequence similarity …