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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Detalles Bibliográficos
Autores principales: Haupt, Melina, Blakeley, Matthew P., Fisher, Stuart J., Mason, Sax A., Cooper, Jon B., Mitchell, Edward P., Forsyth, V. Trevor
Formato: Online Artículo Texto
Lenguaje:English
Publicado: International Union of Crystallography 2014
Materias:
Research Papers
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4224461/
https://www.ncbi.nlm.nih.gov/pubmed/25485123
http://dx.doi.org/10.1107/S2052252514021113

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4224461/
https://www.ncbi.nlm.nih.gov/pubmed/25485123
http://dx.doi.org/10.1107/S2052252514021113

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