Many proteins and protein segments cannot attain a single stable three-dimensional
structure under physiological conditions; instead, they adopt multiple interconverting …

The facts that many proteins with crucial biological functions do not have unique structures
and that many biological processes are compartmentalized into the liquid-like biomolecular …

Intrinsically disordered proteins (IDPs) and regions (IDRs) are commonly found in all
proteomes analyzed so far. These proteins/regions are subject to numerous …

Motivation The identification of binding hotspots in protein–RNA interactions is crucial for
understanding their potential recognition mechanisms and drug design. The experimental …

Proteins from the intrinsically disordered group (IDP) focus the attention of many researchers
engaged in protein structure analysis. The main criteria used in their identification are lack of …

Intrinsically disorder regions (IDRs) are abundant in nature, particularly among Eukaryotes.
While they facilitate a wide spectrum of cellular functions including signaling, molecular …

The nuclear-cytoplasmic transport of biomolecules is assisted by the nuclear pores
composed of evolutionarily conserved proteins termed nucleoporins (Nups). The central …

Hot spot residues at protein–RNA complexes are vitally important for investigating the
underlying molecular recognition mechanism. Accurately identifying protein–RNA binding …

Intrinsically disordered proteins (IDPs) participate in many biological processes by
interacting with other proteins, including the regulation of transcription, translation, and the …

Background DNA-binding proteins perform important roles in cellular processes and are
involved in many biological activities. These proteins include crucial protein-DNA binding …