Large contact surfaces of protein–protein interactions (PPIs) remain to be an ongoing issue
in the discovery and design of small molecule modulators. Peptides are intrinsically capable …

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 …

Hot spots are the subset of interface residues that account for most of the binding free
energy, and they play essential roles in the stability of protein binding. Effectively identifying …

Experimental detection of residues critical for protein-protein interactions (PPI) is a
timeconsuming, costly, and labor-intensive process. Hence, high-throughput PPI-hot spot …

Most biological processes involve multiple proteins interacting with each other. It has been
recently discovered that certain residues in these protein-protein interactions, which are …

Proteins are not isolated biological molecules, which have the specific three-dimensional
structures and interact with other proteins to perform functions. A small number of residues …

Single-point mutations of certain residues (so-called hot spots) impair/disrupt protein–
protein interactions (PPIs), leading to pathogenesis and drug resistance. Conventionally, a …

Protein–protein interactions (PPIs) are emerging as attractive targets for drug design
because of their central role in directing normal and aberrant cellular functions. These …

Receptor‐based QSAR approaches can enumerate the energetic contributions of amino
acid residues toward ligand binding only when experimental binding affinity is associated …

Protein-protein interactions govern almost all biological processes and the underlying
functions of proteins. The interaction sites of protein depend on the 3D structure which in …