Ontology highlight
ABSTRACT:
SUBMITTER: Feige MJ
PROVIDER: S-EPMC2533197 | biostudies-literature | 2008 Sep
REPOSITORIES: biostudies-literature
Feige Matthias J MJ Groscurth Sandra S Marcinowski Moritz M Yew Zu Thur ZT Truffault Vincent V Paci Emanuele E Kessler Horst H Buchner Johannes J
Proceedings of the National Academy of Sciences of the United States of America 20080903 36
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 were able to trap the intermediate in equilibrium and characterize it at atomic resolu ...[more]