Pathogenic Mutations Induce Partial Structural Changes in Native β-Sheet Structure of Transthyretin and Accelerate Aggregation

Amyloid formation of natively folded proteins involves global and/or local unfolding of the native state to form aggregation-prone intermediates. Here we report solid-state NMR structural studies of amyloid derived from wild-type (WT) and more aggressive mutant forms of transthyretin (TTR) to invest...

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Vydáno v:Biochemistry
Hlavní autoři: Lim, Kwang Hun, Dasari, Anvesh K. R., Ma, Renze, Hung, Ivan, Gan, Zhehong, Kelly, Jeffery W., Fitzgerald, Michael C.
Médium: Artigo
Jazyk:Inglês
Vydáno: 2017
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On-line přístup:https://ncbi.nlm.nih.gov/pmc/articles/PMC5745580/
https://ncbi.nlm.nih.gov/pubmed/28820582
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/acs.biochem.7b00658
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