Heat shock protein 90 (Hsp90) is a dimeric molecular chaperone essential for the maturation and folding of a large set of different client proteins. In this project, we will use single molecule experiments to study the mechanics and dynamics that Hsp90 undergoes, especially in the presence of nucleotides, co-chaperones and clients. Together with biochemical and in vivo experiments this will provide detailed insights into the conformational regulation of the Hsp90 machinery and how it chaperones its clients.
DFG Programme
Collaborative Research Centres
