个人简介

National Institute of Health Career Award, 2005 38th Eastern Analytical Symposium Prize, 1999

研究领域

Chemical Biology/Environmental & Green Chemistry/Chemical Physics/Experimental Physical Chemistry/

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)

近期论文

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Vostrikov V., Soller K., Ha K., Gopinath T., Veglia G. Effects of naturally occuring arginine 14 deletion on phospholamban conformational dynamics and membrane interactions. Biochim. Biophys. Acta 2015, 1848, 315. Srivastava A., McDonald L., Cembran A., Kim J., Masterson L., McClendon C., Taylor S., Veglia G. Synchronous opening and closing motions are essential for cAMP-dependent protein kinase A signaling. Structure 2014, 22, 1735. Cero C., Vostrikov V., Verardi R., Severini C., Gopinath T., Braun P., Sassano M., Gurney A., Roth B., Vulchanova L., Possenti R., Veglia G., Bartolomucci A. The TLQP-21 peptide activates the G-protein-coupled receptor C3aR1 via a folding-upon-binding mechanism. Structure 2014, 22, 1744. De Simone A., Mote K., Veglia G. Structural dynamics and conformational equilibria of SERCA regulatory proteins in membranes by solid-state NMR restrained simulations. Biophys J. 2014, 12, 2566. Chao F., Kim J., Xia Y., Milligan M., Rowe N., Veglia G. FLAMEnGO 2.0: An enhanced fuzzy logic algorithm for structure-based assignment of methyl group resonances. J. Magn. Reson. 2014, 245, 17-23. 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. Vostrikov V., Veglia G. Structural topologies of phosphorylated and non-phosphorylated oligomeric phospholamban in lipid membranes by a hybrid NMR approach. Advances in Biological Solid-State NMR: Proteins and Membrane-Active Peptides 2014, Chapter 22, 425-43. Jing M., Verardi R., Veglia G., Bowser M. Development of a sensitive assay for SERCA activity using FRET detection of ADP. Anal. Methods 2014, 6, 1468-1474. Cembran A., Kim J., Gao J., Veglia G. NMR mapping of protein conformational landscapes using coordinated behavior of chemical shifts upon ligand binding. Phys. Chem. Chem. Phys. 2014, 16, 6508-6518. Vostrikov V.V., Mote K.R., Verardi R., Veglia G. Structural dynamics and topology of phosphorylated phospholamban homopentamer reveal its role in the regulation of calcium transport. Structure 2013, 21, 2119-2130. 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. Eggimann B., Vostrikov V.V., Veglia G., Siepmann I. Modeling helical proteins using residual dipolar couplings, sparse long-range distance constraints and a simple residue-based force field. Theor. Chem. Acc. 2013, 132, 1388 Porcelli F., Ramamoorthy A., Barany G., Veglia G. On the role of NMR spectroscopy for characterization of antimicrobial peptides. Methods Mol. Biol. 2013, 1063, 159-180 De Simone A., Gustavsson M., Montalvao R.W., Shi L., Veglia G., Vendruscuolo M. Structures of the excited states of phospholamban and shifts in their populations upon phosphorylation. Biochemistry 2013, 52, 6684-6694 Mote K.R., Gopinath T., Veglia G. Determination of structural topology of a membrane protein in lipid bilayers using polarization optimized experiments (POE) for static and MAS solid state NMR spectroscopy. J. Biomol. NMR. 2013, 57, 91-102 Gopinath T., Mote K.R., Veglia G. Sensitivity and resolution enhancement of oriented solid-state NMR: Application to membrane proteins. Prog. Nucl. Magn. Reson. Spectrosc. 2013, 75, 50-68 Veglia G., Cembran A. Role of conformational entropy in the activity and regulation of the catalytic subunit of protein kinase A. FEBS. J. 2013, 280, 5608-5615 Gopinath T., Veglia G. Orphan spin operators enable the acquisition of multiple 2D and 3D magic angle spinning solid-state NMR spectra. J. Chem. Phys. 2013, 138, 184201 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 Veglia G., Traaseth N.J., Shi. L., Verardi R., Gopinath T., Gustavsson M. The Hybrid Solution/Solid-State NMR Method for Membrane Protein Structure Determination. Comprehensive Biophysics. 2012, 1, 182-198