The diversity of molecular interactions involving intrinsically disordered proteins: A molecular modeling perspective

Intrinsically Disordered Proteins and Regions (IDPs/IDRs) are key components of a multitude biological processes. Conformational malleability enables IDPs/IDRs to perform very specialized functions that cannot be accomplished by globular proteins. The functional role for most these proteins is related the recognition other biomolecules regulate processes or as part signaling pathways. Depending on extent disorder, number interacting sites type partner, different architectures resulting assemblies possible. More recently, molecular condensates with liquid-like properties composed multiple copies IDPs nucleic acids have been proven in eukaryotic cells. structural kinetic details disordered biomolecular complexes difficult unveil experimentally due their inherent conformational heterogeneity. Computational approaches, alone combination experimental data, emerged unavoidable tools understand mechanisms this elusive assemblies. level description used, all-atom coarse-grained, strongly depends size systems timescale investigated mechanism. In mini-review, we describe relevant found interactions involving computational strategies applied investigation.