Misfolded proteins are capable of forming tree-like aggregates in Alzheimer's disease

A method by Rice University researchers to model the way proteins fold - and sometimes misfold - has revealed branching behavior that may have implications for Alzheimer's and other aggregation diseases.Results from the research appear online in the Proceedings of the National Academy of Sciences.In an earlier study of the muscle protein titin, Rice chemist Peter Wolynes and his colleagues analyzed the likelihood of misfolding in proteins, in which domains - discrete sections of a protein with independent folding characteristics - become entangled with like sequences on nearby chains.

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