Alteration of the α-Synuclein Folding Landscape by a Mutation Related to Parkinson's Disease

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 (s...

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Bibliographic Details
Published in:Angewandte Chemie (International ed.) 2010-05, Vol.49 (20), p.3469-3472
Main Authors: Ferreon, Allan Chris M, Moran, Crystal R, Ferreon, Josephine C, Deniz, Ashok A
Format: Article
Language:English
Subjects:
alpha-Synuclein - chemistry
alpha-Synuclein - genetics
alpha-Synuclein - metabolism
Circular Dichroism
Communication
conformational switching
FRET
Models, Molecular
Mutation
Parkinson Disease - genetics
Parkinson Disease - metabolism
Protein Folding
Protein Structure, Secondary
single-molecule biophysics
Thermodynamics
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Summary: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.
ISSN:1433-7851
1521-3773
DOI:10.1002/anie.201000378