Kim, H. Y.Cho, M. K.Kumar, A.Maier, E.Siebenharr, C.Becker, S.Fernandez, C. O.Lashuel, H. A.Benz, R.Lang, A.Zweckstetter, M.2009-10-292009-10-292009-10-29200910.1021/ja9077599https://infoscience.epfl.ch/handle/20.500.14299/44021WOS:000272207300076Soluble oligomers are potent toxins in many neurodegenerative diseases, but little is known about the structure of soluble oligomers and their structure-toxicity relationship. Here we prepared on-pathway oligomers of the 140-residue protein alpha-synuclein, a key player in Parkinson's disease, at concentrations an order of magnitude higher than previously possible. The oligomers form ion channels with well-defined conductance states in a variety of membranes, and their beta-structure differs from that of amyloid fibrils of alpha-synuclein.Amyloid Beta-PeptideSolid-State NmrAlzheimers-DiseaseNeurodegenerative DiseaseFlavonoid BaicaleinSecondary StructureProteinFibrilsChannelsDynamicstext::journal::journal article::research article