The overall goal of my group is to study the structure and dynamics of membrane embedded enzymes. We use a multidisciplinary approach, which includes molecular biology, multidimensional solution and solid-state NMR spectroscopy, and molecular modeling. Recently, we are focusing on the development of new spectroscopic methods to study the interactions between membrane embedded proteins. An application of these new techniques is illustrated in the Figure on the right, where we studied a complex phospholamban and Ca-ATPase (Zamoon et al. PNAS, in press)
Vostrikov V., Soller K., Ha K., Gopinath T., Veglia G. Effects of naturally occurring arginine 14 deletion on phospholamban conformational dynamics and membrane interactions. Biochim. Biophys. Acta 2014, DOI: 10.1016/j.bbamem.2014.09.007
Fusco G., De Simone A., Gopinath T., Vostrikov V., Vendruscolo M., Dobson C., Veglia G. Direct observation of the three regions in α-synuclein that determine its membrane-bound behaviour. Nat. Commun. 2014, 5, 3827
Gustavsson M., Verardi R., Mullen D.G., Mote K.R., Traaseth N.J., Gopinath T., Veglia G. Allosteric regulation of SERCA by phosphorylation-mediated conformational shift of phospholamban. Proc. Natl. Acad. Sci. USA 2013, 110, 17338-17343.
Chao F.A., Morelli A., Haugner 3rd J.C., Churchfield L., Hagmann L.N., Shi L., Masterson L.R., Sarangi R., Veglia G., Seelig B. Structure and dynamics of a primordial catalytic fold generated by in vitro evolution. Nature Chem. Biol. 2013, 9, 81-83