Authors: | Mukherjee, Sanjib K. Knop, Jim-Marcel Möbitz, Simone Winter, Roland |
Title: | Alteration of the conformational dynamics of a DNA hairpin by α-synuclein in the presence of aqueous two-phase systems |
Language (ISO): | en |
Abstract: | The 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. |
Subject Headings: | Biophysics DNA hairpin High pressure chemistry smFRET a-synuclein |
Subject Headings (RSWK): | Biophysik Haarnadelschleife Hochdruckchemie Fluoreszenz-Resonanz-Energie-Transfer Synuclein <alpha-> |
URI: | http://hdl.handle.net/2003/40342 http://dx.doi.org/10.17877/DE290R-22217 |
Issue Date: | 2020-05-26 |
Rights link: | https://creativecommons.org/licenses/by/4.0/ |
Appears in Collections: | Physikalische Chemie |
Files in This Item:
File | Description | Size | Format | |
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chem.202002119.pdf | 1.25 MB | Adobe PDF | View/Open |
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