Abstract
Aggregation of proteins with expanded polyglutamine tracts is implicated in the onset and progression of nine different neurodegenerative diseases including Huntington's disease. Recent work from our lab has focused on the driving forces for polyglutamine aggregation. We have shown that water is a poor solvent for polyglutamine. We have also shown that non-specific homotypic associations of collapsed albeit disordered polyglutamine molecules are spontaneous (non-nucleated), chain length dependent, and governed by the intrinsic disorder (spontaneous fluctuations) of these molecules.
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