Investigating the function of topological changes in membrane-crossing viral proteins.

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O-linked carbohydrates play an important part in cell adhesion, combating viral infection, and many other important physiological processes. Our lab has recently discovered that a catalyst of disulfide bond formation regulates a set of enzymes in

We have a very exciting new project on the redox-regulation of cell division, with implications for cancer treatment. The project involves biochemistry and structural biology, with the option of visiting a collaborating lab in Europe.

Believe it or not, mucus is one of the most beautiful substances in the world if you look at it at the right resolution. The right resolution is of course in atomic detail. Come help us determine the high-resolution structures of mucus proteins using c

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