{"id":6620,"date":"2016-12-15T09:10:01","date_gmt":"2016-12-15T09:10:01","guid":{"rendered":"http:\/\/www.neurodegenerationresearch.eu\/?p=6620"},"modified":"2016-12-15T09:10:42","modified_gmt":"2016-12-15T09:10:42","slug":"hunt-for-huntingtons-cause-yields-clues","status":"publish","type":"post","link":"https:\/\/neurodegenerationresearch.eu\/hr\/2016\/12\/hunt-for-huntingtons-cause-yields-clues\/","title":{"rendered":"Hunt for Huntington\u2019s Disease Cause Yields Clues"},"content":{"rendered":"

Scientists have uncovered new details about how a repeating nucleotide sequence in the gene for a mutant protein may trigger Huntington\u2019s and other neurological diseases.<\/p>\n

Researchers used computer models to analyze proteins suspected of misfolding and forming plaques in the brains of patients with neurological diseases. Their simulations confirmed experimental results by other labs that showed the length of repeating polyglutamine sequences contained in proteins is critical to the onset of disease.<\/p>\n

The study appears in the Journal of the American Chemical Society<\/em>.<\/p>\n

Glutamine is the amino acid coded for by the genomic trinucleotide CAG. Repeating glutamines, called polyglutamines, are normal in huntingtin proteins, but when the DNA is copied incorrectly, the repeating sequence of glutamines can become too long. The result can be diseases like Huntington\u2019s or spinocerebellar ataxia.<\/p>\n

Aggregation in Huntington\u2019s typically begins only when polyglutamine chains reach a critical length of 36 repeats. Studies have demonstrated that longer repeat chains can make the disease more severe and its onset earlier.<\/p>\n

The researchers\u2019 simulations showed how sequences with 30 repeats or more are able to fold by themselves without partners into hairpin shapes, which are the building blocks for troublesome aggregates. Thus, for the longer sequences, even a single protein can begin the aggregation process, especially at high concentrations.<\/p>\n

The research team also found that at intermediate lengths between 20 and 30 repeats, polyglutamine<\/a> sequences can choose between straight or hairpin configurations. While longer and shorter sequences form aligned fiber bundles, simulations showed intermediate sequences are more likely to form disordered, branched structures.<\/p>\n

The team\u2019s ongoing study is now looking at how the complete huntingtin protein, which contains parts in addition to the polyglutamine repeats, aggregates.
\n
\nPaper: \u201cThe Aggregation Free Energy Landscapes of Polyglutamine Repeats\u201d<\/a>
\nReprinted from materials provided by Rice University<\/a>. <\/strong><\/p>\n","protected":false},"excerpt":{"rendered":"

Scientists have uncovered new details about how a repeating nucleotide […]<\/p>\nView Post<\/a>","protected":false},"author":3,"featured_media":4999,"comment_status":"closed","ping_status":"closed","sticky":false,"template":"","format":"standard","meta":{"_acf_changed":false,"footnotes":""},"categories":[22],"tags":[],"class_list":["post-6620","post","type-post","status-publish","format-standard","has-post-thumbnail","hentry","category-research-news"],"acf":[],"yoast_head":"\nHunt for Huntington\u2019s Disease Cause Yields Clues - JPND Neurodegenerative Disease Research<\/title>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" href=\"https:\/\/neurodegenerationresearch.eu\/it\/2016\/12\/hunt-for-huntingtons-cause-yields-clues\/\" \/>\n<meta property=\"og:locale\" content=\"hr_HR\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"Hunt for Huntington\u2019s Disease Cause Yields Clues - 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