Ontology highlight
ABSTRACT:
SUBMITTER: Jahn M
PROVIDER: S-EPMC4273377 | biostudies-literature | 2014 Dec
REPOSITORIES: biostudies-literature
Jahn Markus M Rehn Alexandra A Pelz Benjamin B Hellenkamp Björn B Richter Klaus K Rief Matthias M Buchner Johannes J Hugel Thorsten T
Proceedings of the National Academy of Sciences of the United States of America 20141202 50
The heat shock protein 90 (Hsp90) is a dimeric molecular chaperone essential in numerous cellular processes. Its three domains (N, M, and C) are connected via linkers that allow the rearrangement of domains during Hsp90's chaperone cycle. A unique linker, called charged linker (CL), connects the N- and M-domain of Hsp90. We used an integrated approach, combining single-molecule techniques and biochemical and in vivo methods, to study the unresolved structure and function of this region. Here we ...[more]