Multitude NMR studies of α-synuclein familial mutants: probing their differential aggregation propensities.
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DOI: 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… read more here.
Keywords: nmr studies; aggregation; multitude nmr; synuclein familial ... See more keywords