Mukherjee, Sanjib K.Knop, Jim-MarcelMöbitz, SimoneWinter, Roland2021-07-292021-07-292020-05-26http://hdl.handle.net/2003/4034210.17877/DE290R-22217The effect of an amyloidogenic intrinsically disordered protein, α-synuclein, which is associated with Parkinson's disease (PD), on the conformational dynamics of a DNA hairpin (DNA-HP) was studied by employing the single-molecule Förster resonance energy transfer method. The open-to-closed conformational equilibrium of the DNA-HP is drastically affected by binding of monomeric α-synuclein to the loop region of the DNA-HP. Formation of a protein-bound intermediate conformation is fostered in the presence of an aqueous two-phase system mimicking intracellular liquid-liquid phase separation. Using pressure modulation, additional mechanistic information about the binding complex could be retrieved. Hence, in addition to toxic amyloid formation, α-synuclein may alter expression profiles of disease-modifying genes in PD. Furthermore, these findings might also have significant bearings on the understanding of the physiology of organisms thriving at high pressures in the deep sea.enChemistry - a european journal;Vol. 26. 2020, issue 48, pp 10987-10991https://creativecommons.org/licenses/by/4.0/BiophysicsDNA hairpinHigh pressure chemistrysmFRETa-synuclein540article (journal)BiophysikHaarnadelschleifeHochdruckchemieFluoreszenz-Resonanz-Energie-TransferSynuclein <alpha->