Multiscale Simulations Elucidate the Mechanism of Polyglutamine Aggregation and the Role of Flanking Domains in Fibril Polymorphism

Protein aggregation, which is implicated in aging and neurodegenerative diseases, typically involves a transition from soluble monomers and oligomers to insoluble fibrils. Polyglutamine (polyQ) tracts in proteins can form amyloid fibrils, which are linked to polyQ diseases, including Huntington’s di...

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Bibliografski detalji
Glavni autor:	Avijeet Kulshrestha (14290812) (author)
Daljnji autori:	Tien Minh Phan (22439576) (author), Azamat Rizuan (13727105) (author), Priyesh Mohanty (11280405) (author), Jeetain Mittal (1281789) (author)
Izdano:	2025
Teme:	Biophysics Biochemistry Medicine Genetics Neuroscience Developmental Biology Computational Biology Biological Sciences not elsewhere classified Chemical Sciences not elsewhere classified Physical Sciences not elsewhere classified Information Systems not elsewhere classified width branched morphologies state polymorphism associated including huntington ’ hybrid multistate structure high computational efficiency despite significant research atomistic information regarding achieving qualitative agreement n17 flanking domain multiscale simulations elucidate form amyloid fibrils structurally stable oligomers ego simulation methodology httex1 amyloid aggregation httex1 aggregation insoluble fibrils flanking domains aggregation simulations amyloid fibrillation simulations reveal simulations based typically involves strand structures strand conformations soluble monomers shown promise neurodegenerative diseases morphological characteristics molecular dynamics intermediate stages incorporating combinations huntingtin protein hd ), chain interdigitation based model
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Multiscale Simulations Elucidate the Mechanism of Polyglutamine Aggregation and the Role of Flanking Domains in Fibril Polymorphism

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