KnowraIntrinsically disordered proteinLinked fromLinked fromThe 13 pages that link to Intrinsically disordered protein, each with the reason it gives.All 13Broader topic 1Related 8Compared with 4Protein foldingCompared with: Some functional proteins do not settle into one stable folded structure.Protein structureCompared with: It challenges the expectation that every functional protein has one stable folded shape.Desiccation toleranceRelated: Many protective proteins only fold or act in the dry state; how they work is unsettled.Protein misfoldingCompared with: Disorder is a normal structural property, not necessarily a folding defect.Structural biologyRelated: Structural methods must account for ensembles rather than one fixed molecular model.TardigradeRelated: Tardigrade-specific disordered proteins have been studied for their role in desiccation tolerance.AnhydrobiosisRelated: Some protect dehydrating cells by forming glass-like matrices or shielding other molecules.Tau proteinRelated: Tau’s flexible structure helps it interact with multiple partners and complicates its aggregation.CytosolRelated: Many such regions remain soluble in cytosol and support transient interactions.CryptobiosisRelated: Tardigrade DSG and SAHS proteins shield other molecules during desiccation.Kurt WüthrichBroader topic: NMR methods developed for solution samples are suited to studying disordered regions.Christian B. AnfinsenCompared with: Such proteins challenge the idea that every sequence specifies one stable native shape.Biomolecular & subcellular processesRelated: Its flexible interactions challenge structure-based accounts of molecular function.