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 …

Proteins may vary from being rigid to having flexible regions to being completely disordered,
either as an intrinsically disordered protein (IDP) or having specific intrinsically disordered …

This is a sequel to the previous Perspective “The CH–π hydrogen bond in chemistry.
Conformation, supramolecules, optical resolution and interactions involving carbohydrates” …

Accurate prediction of standard binding free energies describing protein–ligand association
remains a daunting computational endeavor. This challenge is rooted to a large extent in the …

Many aspects of cell signalling, trafficking, and targeting are governed by interactions
between globular protein domains and short peptide segments. These domains often bind …

Protein–protein interactions are essential in every aspect of cellular activity. Multiprotein
complexes form and dissociate constantly in a specifically tuned manner, often by conserved …

Determination of the binding specificity of SH3 domain, a peptide recognition module (PRM),
is important to understand their biological functions and reconstruct the SH3-mediated …

Heme-binding protein 23 kDa (HBP23), a rat isoform of human proliferation-associated gene
product (PAG), is a member of the peroxiredoxin family of peroxidases, having two …

Although hydrophobic interaction is the main contributing factor to the stability of the protein
fold, the specificity of the folding process depends on many directional interactions. An …

Src-family kinases are modular signaling proteins involved in a diverse array of cellular
processes. All members of the Src family share the same domain organization, with modular …