Intrinsically disordered proteins may escape unwanted interactions via functional misfolding

► IDPs are abundant in nature and have crucial functions. ► They possess remarkable binding promiscuity and can fold at binding to partners. ► They often have transient, interaction prone elements that are used for binding. ► Unbound IDPs can functionally misfold, thus sequestering the preformed elements. ► Functional misfolding prevents IDPs from the unwanted interactions.