Structure Solution of Misfolded Conformations Adopted by Intrinsically Disordered Alzheimer's Tau Protein

Until now it was impossible to obtain atomic structure of intrinsically disordered protein (IDP) tau and/or its assembly in Alzheimer's paired helical filaments as neither of them could have been prepared in the form amenable to Xray or NMR techniques. Using IDP tau property to attain regular tertiary structure after binding events during selfassembly or when complexed with its target we propose monoclonal antibodies as surrogate tau protein binding partners to form complexes and crystals for structure solution by X-ray technique.