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Alteration of the α‐Synuclein Folding Landscape by a Mutation Related to Parkinson’s Disease
Author(s) -
Ferreon Allan Chris M.,
Moran Crystal R.,
Ferreon Josephine C.,
Deniz Ashok A.
Publication year - 2010
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201000378
Subject(s) - parkinson's disease , mutation , alpha synuclein , folding (dsp implementation) , disease , neuroscience , biology , genetics , medicine , evolutionary biology , pathology , engineering , gene , electrical engineering
Shape shifting linked to disease : A single‐molecule fluorescence technique was used to probe structures of an intrinsically disordered brain protein. A mutation was found to tilt the coupled binding–folding energy landscape of the protein and inhibited switching between induced ordered structures (see picture). The observations provide fundamental insight into the molecular basis of Parkinson's disease.