https://www.google.com/search?q=do+IDRs+in+protein+tend+to+be+multifunctional&rlz=1C5CHFA_enUS1047US1048&oq=do+IDRs+in+protein+tend+to+be+multifunctional&gs_lcrp=EgZjaHJvbWUyBggAEEUYOTIHCAEQIRigATIHCAIQIRigATIHCAMQIRigATIHCAQQIRiPAtIBCjExMTAyMWowajeoAgCwAgA&sourceid=chrome&ie=UTF-8 QT:{{” Yes, Intrinsically Disordered Regions (IDRs) in proteins are indeed highly multifunctional, acting as flexible hubs that bind diverse partners, integrate signals, and facilitate complex assembly, offering unique advantages over structured proteins through
context-dependent interactions and phase separation. Their flexibility allows them to adopt multiple conformations (a dynamic ensemble), enabling a single IDR to perform various roles like scaffolding, allosteric regulation, and participation in cellular condensates (LLPS). “}}
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