Thats a unique idea.You should consider the following idea to enhance your idea so that it would impact uniquely: Expansion of polyglutamine (polyQ) tracts in proteins results in protein aggregation and is associated with cell death in at least nine neurodegenerative diseases. Disease age of onset is correlated with the polyQ insert length above a critical value of 35–40 glutamines. The aggregation kinetics of isolated polyQ peptides in vitro also shows a similar critical-length dependence. While recent experimental work has provided considerable insights into polyQ aggregation, the molecular mechanism of aggregation is not ll understood. Here, using computer simulations of isolated polyQ peptides,  show that a mechanism of aggregation is the conformational transition in a single polyQ peptide chain from random coil to a parallel β-helix. This transition occurs selectively in peptides longer than 37 glutamines. In the β-helices observed in simulations, all residues adopt β-strand backbone dihedral angles, and the polypeptide chain coils around a central helical axis with 18.5 ± 2 residues per turn.  also find that mutant polyQ peptides with proline-glycine inserts show formation of antiparallel β-hairpins in their ground state, in agreement with experiments. The lor stability of mutant β-helices explains their lor aggregation rates compared to wild type. Our results provide a molecular mechanism for polyQ-mediated aggregation.
['Sagar D. Khare', 'Feng Ding', 'Kenneth N Gwanmesia', 'Nikolay V. Dokholyan']
I am writing a research paper on a idea Molecular Origin of Polyglutamine Aggregation in Neurodegenerative Diseases
[{"from": "human", "value": "I am writing a research paper on a idea Molecular Origin of Polyglutamine Aggregation in Neurodegenerative Diseases"}, {"from": "gpt", "value": "Thats a unique idea.You should consider the following idea to enhance your idea so that it would impact uniquely: Expansion of polyglutamine (polyQ) tracts in proteins results in protein aggregation and is associated with cell death in at least nine neurodegenerative diseases. Disease age of onset is correlated with the polyQ insert length above a critical value of 35\u201340 glutamines. The aggregation kinetics of isolated polyQ peptides in vitro also shows a similar critical-length dependence. While recent experimental work has provided considerable insights into polyQ aggregation, the molecular mechanism of aggregation is not ll understood. Here, using computer simulations of isolated polyQ peptides,  show that a mechanism of aggregation is the conformational transition in a single polyQ peptide chain from random coil to a parallel \u03b2-helix. This transition occurs selectively in peptides longer than 37 glutamines. In the \u03b2-helices observed in simulations, all residues adopt \u03b2-strand backbone dihedral angles, and the polypeptide chain coils around a central helical axis with 18.5 \u00b1 2 residues per turn.  also find that mutant polyQ peptides with proline-glycine inserts show formation of antiparallel \u03b2-hairpins in their ground state, in agreement with experiments. The lor stability of mutant \u03b2-helices explains their lor aggregation rates compared to wild type. Our results provide a molecular mechanism for polyQ-mediated aggregation."}]