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Issue 29, 2018
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Multitude NMR studies of α-synuclein familial mutants: probing their differential aggregation propensities

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Abstract

Familial mutations in α-synuclein affect the immediate chemical environment of the protein's backbone, changing its aggregation kinetics and forming diverse structural and functional intermediates. This study, concerning two oppositely aggregating mutants A30P and E46K, reveals a completely diverse conformational landscape for each, thus providing atomistic insights into differences in their aggregation dynamics.

Graphical abstract: Multitude NMR studies of α-synuclein familial mutants: probing their differential aggregation propensities

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Publication details

The article was received on 18 Dec 2017, accepted on 20 Feb 2018 and first published on 20 Feb 2018


Article type: Communication
DOI: 10.1039/C7CC09597J
Citation: Chem. Commun., 2018,54, 3605-3608
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    Multitude NMR studies of α-synuclein familial mutants: probing their differential aggregation propensities

    D. Bhattacharyya, R. Kumar, S. Mehra, A. Ghosh, S. K. Maji and A. Bhunia, Chem. Commun., 2018, 54, 3605
    DOI: 10.1039/C7CC09597J

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