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

Bhattacharyya, Dipita ; Kumar, Rakesh ; Mehra, Surabhi ; Ghosh, Anirban ; Maji, Samir K. ; Bhunia, Anirban (2018) Multitude NMR studies of α-synuclein familial mutants: probing their differential aggregation propensities Chemical Communications, 54 (29). pp. 3605-3608. ISSN 1359-7345

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Official URL: http://doi.org/10.1039/C7CC09597J

Related URL: http://dx.doi.org/10.1039/C7CC09597J

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.

Item Type:Article
Source:Copyright of this article belongs to Royal Society of Chemistry
ID Code:126464
Deposited On:31 Oct 2022 04:13
Last Modified:31 Oct 2022 04:13

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