Rich data bearing on the structural and evolutionary principles of protein–protein
interactions are paving the way to a better understanding of the regulation of function in the …

Many proteins have small-molecule binding pockets that are not easily detectable in the
ligand-free structures. These cryptic sites require a conformational change to become …

Recent studies found that membrane-bound K-Ras dimers are important for biological
function. However, the structure and thermodynamic stability of these complexes remained …

Highlights•Specificity and stability are two major determinants of protein recognition in
transient protein–protein complexes (tPPCs).•Some interface residues of tPPCs are rigid in …

Resistance mutations in Mycobacterium tuberculosis (Mtb) catalase peroxidase protein
(KatG), an essential enzyme in isoniazid (INH) activation, reduce the sensitivity of Mtb to first …

Activation of the inflammasome is accompanied by rapid formation of a micrometer-sized
perinuclear structure called the ASC speck, a platform for caspase-1 activity. The ASC speck …

Background Determining protein-protein interactions and their binding affinity are important
in understanding cellular biological processes, discovery and design of novel therapeutics …

Proteins are extremely heterogenous molecules, which allows them to execute such a large
variety of biological functions. Proteins have structural roles, perform chemical catalysis and …

Background Protein-protein interactions are crucial for normal biological processes and to
regulate cellular reactions that affect gene expression and function. Several previous studies …

Motivation: B-cell epitope is a small area on the surface of an antigen that binds to an
antibody. Accurately locating epitopes is of critical importance for vaccine development …