Untangling the interaction of α-synuclein with DNA i-motifs and hairpins by volume-sensitive single-molecule FRET spectroscopy.
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ABSTRACT:
SUBMITTER: Mukherjee SK
PROVIDER: S-EPMC8341996 | biostudies-literature | 2021 Aug
REPOSITORIES: biostudies-literature
Publications
Untangling the interaction of α-synuclein with DNA i-motifs and hairpins by volume-sensitive single-molecule FRET spectroscopy.
Mukherjee Sanjib K SK Knop Jim-Marcel JM Oliva Rosario R Möbitz Simone S Winter Roland R
RSC chemical biology 20210702 4
The intrinsically disordered protein α-synuclein causes Parkinson's disease by forming toxic oligomeric aggregates inside neurons. Single-molecule FRET experiments revealed conformational changes of noncanonical DNA structures, such as i-motifs and hairpins, in the presence of α-synuclein. Volumetric analyses revealed differences in binding mode, which is also affected by cellular osmolytes. ...[more]
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