Amnon Horovitzamnon.email@example.com Phone: +972-8-934-3399 Homepage of Amnon Horovitz, Opens in new window
Talented and motivated student who wishes to study allostery and function in eukaryotic chaperonins and their connection to various diseases
Ron Diskinron.firstname.lastname@example.org Phone: +972-8-934-6720 Homepage of Ron Diskin, Opens in new window
Investigating the function of topological changes in membrane-crossing viral proteins.[Read more] about Ron Diskin
Please contact for additional details
Rina Rosenzweigrina.email@example.com Phone: +972-8-934-2516 Homepage of Rina Rosenzweig, Opens in new window
NMR studies of transient chaperone-substrate interactions[Read more] about Rina Rosenzweig
Almost all proteins depend on a well-defined three-dimensional structure to obtain their functionality. In order to prevent misfolding, aggregation, and the generation of toxic species, the process of protein folding in the cell is often guided by molecular chaperones. These complex protein networks either interact with substrate polypeptides to help them fold; unfold misfolded species; dissolve aggregates; or deliver substrates to proteolysis. Very little structural information, however, is available regarding how chaperones bind their substrates or the manner in which they protect proteins from misfolding and aggregation.
This lack of information arises from the highly dynamic nature of chaperone-substrate complexes – a trait that prevents their characterization by traditional structural techniques, but fortunately for us, makes them great targets for NMR spectroscopy.
In this project we will use solution-state NMR to probe the molecular interactions between hundreds-of-kilodalton large chaperone complexes and “client” proteins, as well as the structural and dynamic features of these complexes