Ontology highlight
ABSTRACT:
SUBMITTER: Jahn M
PROVIDER: S-EPMC4747692 | biostudies-literature | 2016 Feb
REPOSITORIES: biostudies-literature
Jahn Markus M Buchner Johannes J Hugel Thorsten T Rief Matthias M
Proceedings of the National Academy of Sciences of the United States of America 20160119 5
Folding of small proteins often occurs in a two-state manner and is well understood both experimentally and theoretically. However, many proteins are much larger and often populate misfolded states, complicating their folding process significantly. Here we study the complete folding and assembly process of the 1,418 amino acid, dimeric chaperone Hsp90 using single-molecule optical tweezers. Although the isolated C-terminal domain shows two-state folding, we find that the isolated N-terminal as w ...[more]