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- W2059527306 abstract "The misfolding of the protein α-synuclein (αS) has been implicated in the molecular chain of events leading to Parkinson disease. Physiologically, αS undergoes a transition from a random coil to helical conformation upon encountering synaptic vesicle membranes. On analogous small unilamellar vesicles (SUVs), the conformation of αS is dominated by a single elongated αS helix. However, alternative broken helix states have been postulated, mandating experimental clarification. Here, the upper limit for the free energy difference between elongated and broken helix conformations on SUVs resembling synaptic vesicles was determined to be 1.2 ± 0.4 kcal/mol, which amounts to a population ratio of 7.6:1 between both states (12% broken helices). In response to helix breaks at different positions, αS rearranged in an opportunistic manner, thereby minimizing helix abrogations to as little as one to two turns. Enthalpy and entropy measurements of gel state SUV-αS interactions indicated that broken helix states retain the ability to relieve membrane-packing stress. Thus, broken helix states are a distinct physiological feature of the vesicle-bound αS state, making it a checkered protein of multiple parallel conformations. A continuous interconversion between structural states may contribute to pathological αS misfolding." @default.
- W2059527306 created "2016-06-24" @default.
- W2059527306 creator A5028480003 @default.
- W2059527306 creator A5053880652 @default.
- W2059527306 date "2011-06-01" @default.
- W2059527306 modified "2023-09-27" @default.
- W2059527306 title "α-Synuclein Populates Both Elongated and Broken Helix States on Small Unilamellar Vesicles" @default.
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- W2059527306 doi "https://doi.org/10.1074/jbc.m111.224055" @default.
- W2059527306 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3122204" @default.
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- W2059527306 hasPublicationYear "2011" @default.
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