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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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| Pubblicato in: | IUCrJ |
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| Autori principali: | , , , , , , |
| Natura: | Artigo |
| Lingua: | Inglês |
| Pubblicazione: |
International Union of Crystallography
2014
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| Soggetti: | |
| 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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