Alteration of the α-svnuclein folding landscape by a mutation related to Parkinson's disease

Abstract

(Figure Presented). Shape shifting linked to disease: A singlemolecule 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. © 2010 Wiley-VCH Verlag GmbH & Co. KGaA.