Intrinsically disordered proteins (IDPs) display a large number of interaction modes
including folding-upon-binding, binding without major structural transitions, or binding …

We introduce computational studies on intrinsically disordered proteins (IDPs). Especially,
we present our multicanonical molecular dynamics (McMD) simulations of two IDP-partner …

Zika virus (ZIKV) is a global health concern and has been linked to severe neurological
pathologies. Although no medication is available yet, many efforts to develop antivirals and …

The notion that protein function relies on a precise 3D structure constitutes one of the central
paradigms of biochemistry. According to this concept, a protein can perform its biological …

The nuclear factor erythroid 2-related factor 2 (Nrf2) protein is a critical transcription factor for
activating the antioxidant response pathway, a primary defense mechanism against …

Exploring at the molecular level, all possible ligand–protein approaching pathways and,
consequently, identifying the energetically favorable binding sites is considered crucial to …

The nuclear receptor superfamily (NR), as a major group of intracellular receptors, regulate
broad aspects of cell functions. The activation of these receptors is regulated by …

Highlights•Intrinsically disordered proteins (IDPs) employ a variety of binding
mechanisms.•They may form stable folded complex structures or remain highly …

Coupled binding and folding is frequently involved in specific recognition of so‐called
intrinsically disordered proteins (IDPs), a newly recognized class of proteins that rely on a …

Intrinsically disordered proteins (IDPs) lack a well-defined tertiary structure but are essential
players in various biological processes. Their ability to undergo a disorder-to-order transition …