期刊
CHEMICAL COMMUNICATIONS
卷 54, 期 29, 页码 3605-3608出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c7cc09597j
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资金
- Council of Scientific and Industrial Research (CSIR), Govt. of India [02(0292)/17/EMR-II]
- CSIR-UGC, Govt. of India
Familial mutations in alpha-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.
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