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...

Descripción completa

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

Internet

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

Ejemplares similares