NMR Metabolomics
Now that Google and CryoEM have solved protein folding (well as far as granting agencies are concerned -BTW, protein folding has been “solved” at least 5 times in my career before) we’re getting into some new stuff. Will update when we have more results.
Amyloids
We are examining the structures of fibrils, intermediates in fibril formation, and the role of cofactors in fibrils. Our four model systems are Amylin (type 2 diabetes), Ab (Alzheimer’s Disease), a-synuclein (Parkinson’s Disease), and SEVI (HIV infectivity).
Click here to download long PDF description
NMR protein structure determination
We are still quite active in NMR structure determination, although most of our recent work in this area has been through collaborations. We collaborated with the Dan Gage lab at UConn on the structure of Sma0114, a response regulator that effects signal transduction in S. Melitoti. We collaborated with Prof. Rich Olson from Wesleyan, on the NMR structure of the C-terminal domain of the hemolysin II pore-forming toxin. We have an ongoing extensive collaboration with Prof. Carol Teschke’s lab at UConn on NMR of phage proteins, where we are studying at least three different proteins involved in capsid structure and assembly of dsDNA tailed phages.
Click here to go to the structures our group has solved in the Protein Data Bank (PDB)
Protein Folding
We are interested in the structural characterization of equilibrium folding intermediates. Our long term goal is to use information from experimental protein folding studies to develop improved structure modeling methods.