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- W3034164977 abstract "As an intrinsically disordered protein, monomeric alpha-synuclein (aSyn) occupies a large conformational space. Certain conformations lead to aggregation prone and non-aggregation prone intermediates, but identifying these within the dynamic ensemble of monomeric conformations is difficult. Herein, we used the biologically relevant calcium ion to investigate the conformation of monomeric aSyn in relation to its aggregation propensity. We observe that the more exposed the N-terminus and the beginning of the NAC region of aSyn are, the more aggregation prone monomeric aSyn conformations become. Solvent exposure of the N-terminus of aSyn occurs upon release of C-terminus interactions when calcium binds, but the level of exposure and aSyn's aggregation propensity is sequence and post translational modification dependent. Identifying aggregation prone conformations of monomeric aSyn and the environmental conditions they form under will allow us to design new therapeutics targeted to the monomeric protein." @default.
- W3034164977 created "2020-06-12" @default.
- W3034164977 creator A5002495531 @default.
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- W3034164977 date "2020-06-04" @default.
- W3034164977 modified "2023-10-16" @default.
- W3034164977 title "Extent of N-terminus exposure of monomeric alpha-synuclein determines its aggregation propensity" @default.
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- W3034164977 doi "https://doi.org/10.1038/s41467-020-16564-3" @default.
- W3034164977 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/7272411" @default.
- W3034164977 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/32499486" @default.
- W3034164977 hasPublicationYear "2020" @default.
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