Ontology highlight
ABSTRACT:
SUBMITTER: Ahmad B
PROVIDER: S-EPMC3289313 | biostudies-literature | 2012 Feb
REPOSITORIES: biostudies-literature
Ahmad Basir B Chen Yujie Y Lapidus Lisa J LJ
Proceedings of the National Academy of Sciences of the United States of America 20120127 7
We hypothesize that the first step of aggregation of disordered proteins, such as α-synuclein, is controlled by the rate of backbone reconfiguration. When reconfiguration is fast, bimolecular association is not stable, but as reconfiguration slows, association is more stable and subsequent aggregation is faster. To investigate this hypothesis, we have measured the rate of intramolecular diffusion in α-synuclein, a protein involved in Parkinson's disease, under solvent conditions that accelerate ...[more]