NMR protein structure determination
We are still active in NMR structure determination, mostly having to do with our recent interests in atypical zinc fingers that Google PDB Coordinate Recognition Fold either gets wrong or misses the point with. Prior to Alpha Fold we completed collaborations with the Dan Gage lab at UConn on the structure of Sma0114, a response regulator that affects 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 had an extensive collaboration with Prof. Carol Teschke’s lab at UConn on NMR of several phage proteins.
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 for the basic science sake of understanding the process.
Click here to download long PDF description
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 biophysics 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).