Transient helices with functional roles

Abstract

Intrinsically disordered regions (IDRs) of proteins contribute to various cellular functions, including signal transduction, gene regulation, and subcellular organization (1). One of the most important aspects of IDRs is their contribution to biomolecular condensate formation within cells. IDRs can undergo multivalent intermolecular interactions that drive phase separation. For the multivalent interactions, IDRs may have preferential interaction sites ('stickers') flanked by inert sequences ('spacers') (1). However, how these interactions occur between conformationally flexible polypeptide chains is not well understood.