Article
The structure of a folding intermediate provides insight into differences in immunoglobulin amyloidogenicity.
Proceedings of the National Academy of Sciences of the United States of America - 9 Sept 2008
Feige Matthias J, Groscurth Sandra, Marcinowski Moritz, Yew Zu Thur, Truffault Vincent, Paci Emanuele, Kessler Horst, Buchner Johannes
Abstract excerpt
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 antibody domain to characterize its major folding intermediate in detail. Furthermore, by a single point mutation we...
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