Identification of an aggregation-prone structure of tau.

ABSTRACT: The aggregation and deposition of normally soluble proteins is the hallmark of several devastating neurodegenerative disorders. For proteins such as tau in Alzheimer's disease and α-synuclein in Parkinson's disease, aggregation involves a transition from an intrinsically disordered monomer to a highly structured fiber. While understanding the role of these proteins in neurodegeneration requires elucidation of the structural basis of self-association, the conformational heterogeneity of disordered proteins makes their structural characterization inherently challenging. Here we use single molecule Förster resonance energy transfer to measure the conformational ensemble of tau in the absence and presence of heparin to identify critical conformational changes relevant to the initiation of aggr

SUBMITTER: Elbaum-Garfinkle S 

PROVIDER: S-EPMC3477793 | biostudies-literature | 2012 Oct

REPOSITORIES: biostudies-literature