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Binding site asymmetry in human transthyretin: insights from a joint neutron and X-ray crystallographic analysis using perdeuterated protein

Human transthyretin has an intrinsic tendency to form amyloid fibrils and is heavily implicated in senile systemic amyloidosis. Here, detailed neutron structural studies of perdeuterated transthyretin are described. The analyses, which fully exploit the enhanced visibility of isotopically replaced h...

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Dettagli Bibliografici
Pubblicato in:IUCrJ
Autori principali: Haupt, Melina, Blakeley, Matthew P., Fisher, Stuart J., Mason, Sax A., Cooper, Jon B., Mitchell, Edward P., Forsyth, V. Trevor
Natura: Artigo
Lingua:Inglês
Pubblicazione: International Union of Crystallography 2014
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Accesso online:https://ncbi.nlm.nih.gov/pmc/articles/PMC4224461/
https://ncbi.nlm.nih.gov/pubmed/25485123
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1107/S2052252514021113
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