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Effect of amino acid mutations on the conformational dynamics of amyloidogenic immunoglobulin light-chains: A combined NMR and in silico study

The conformational dynamics of a pathogenic κ4 human immunoglobulin light-chain variable domain, SMA, associated with AL amyloidosis, were investigated by (15)N relaxation dispersion NMR spectroscopy. Compared to a homologous light-chain, LEN, which differs from SMA at eight positions but is non-amy...

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Detalles Bibliográficos
Autores principales:	Mukherjee, Sujoy, Pondaven, Simon P., Hand, Kieran, Madine, Jillian, Jaroniec, Christopher P.
Formato:	Online Artículo Texto
Lenguaje:	English
Publicado:	Nature Publishing Group UK 2017
Materias:	Article
Acceso en línea:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5583243/ https://www.ncbi.nlm.nih.gov/pubmed/28871194 http://dx.doi.org/10.1038/s41598-017-10906-w

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