NMR Spectroscopy and Biochemistry of Proteins

Our research interests are centered on structures of proteins. We are investigating the structure and function of membrane-embedded receptors, in particular those of G-protein coupled receptors. To tackle these challenging targets we have studied fragments comprising large portions (many transmembrane helices) by NMR. Moreover, we have developed a functional mini-receptor capable of mimicking GPCRs based on the beta-barrel membrane protein OmpX. Moreover, we are studying repeat proteins, souble proteins with a repetitive amino acid sequence, in collaboration with groups from the Biochemistry Department, to develop them into binders with predictable binding properties towards unfolded peptides and proteins. Finally, we are interested in protein folding using a combination of site-directed mutagenesis and NMR.
My group uses primarily recombinant methods and protein expression but also solid-phase peptide synthesis to produce the peptides and proteins of interest and high-resolution NMR as well as other biophysical techniques for structurally and functionally characterizing them.