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Article

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

Scientific reports - 4 Sept 2017

Mukherjee Sujoy, Pondaven Simon P, Hand Kieran, Madine Jillian, Jaroniec Christopher P

Abstract excerpt

The conformational dynamics of a pathogenic κ4 human immunoglobulin light-chain variable domain, SMA, associated with AL amyloidosis, were investigated by 15N relaxation dispersion NMR spectroscopy. Compared to a homologous light-chain, LEN, which differs from SMA at eight positions but is non-amyloidogenic in vivo, we find that multiple residues in SMA clustered around the N-terminus and CDR loops experience...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 28871194
DOI: 10.1038/s41598-017-10906-w
PMCID: PMC5583243

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