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Article

Mutation effects on structural stability of polyglutamine peptides by molecular dynamics simulation.

Interdisciplinary sciences, computational life sciences - 1 Mar 2009

Nakano Miki, Watanabe Hirofumi, Starikov E B, Rothstein Stuart M, Tanaka Shigenori

Abstract excerpt

Huntington's disease patients commonly have glutamine (Q) repeats longer than 37 residues in the Huntingtin protein. This unusual protein will misfold and aggregate to form insoluble amyloid-like fibrils. Although the determination of polyQ structure is very important for elucidation of the aggregation mechanism, this has not yet been accomplished due to the experimental difficulties. In this study, we performed...

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Identifiers

PMID: 20640815
DOI: 10.1007/s12539-008-0020-7

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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