The structure of a folding intermediate provides insight into differences in immunoglobulin amyloidogenicity

Folding intermediates play a key role in defining protein folding and assembly pathways as well as those of misfolding and aggregation. Yet, due to their transient nature, they are poorly accessible to high-resolution techniques. Here, we made use of the intrinsically slow folding reaction of an ant...

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Библиографические подробности
Главные авторы: Feige, Matthias J., Groscurth, Sandra, Marcinowski, Moritz, Yew, Zu Thur, Truffault, Vincent, Paci, Emanuele, Kessler, Horst, Buchner, Johannes
Формат: Artigo
Язык:Inglês
Опубликовано: National Academy of Sciences 2008
Предметы:
Biological Sciences
Online-ссылка:https://ncbi.nlm.nih.gov/pmc/articles/PMC2533197/
https://ncbi.nlm.nih.gov/pubmed/18768806
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0802809105
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