Gianluigi Veglia, Principal Investigator

Structure Determination of Membrane Proteins by NMR

This group studied membrane protein structure, dynamics, and interactions with bioactive compounds using nuclear magnetic resonance (NMR) spectroscopy methods. Membrane proteins constitute 15–30% of the genomic sequences and mediate most of the vital cellular activities, functioning as receptors, transporters in channels, and the like. In spite of its biological importance, membrane protein research is lagging behind studies of soluble proteins. This gap will likely be widened by the structural genomic projects. Indeed, conventional structural biology techniques are hampered by the presence of lipids, which are crucial to maintain membrane proteins’ structural and functional integrity. Solution and solid-state NMR methods have emerged as a combined approach to solve the structure of membrane proteins in lipid environments. Using solution NMR methods, it is possible to determine the structure of small and medium-sized membrane proteins in detergent micelles.

Solid-state NMR techniques offer precious information on membrane protein topology and organization in lipid bilayers and promise to be an independent method for structure determination. To obtain the final structures, the NMR data are modeled by using computational methods such as simulated annealing and molecular dynamics calculations. This group is using cns, xplor, and other programs for structural analysis such as PROPCHECK-NMR and AQUA.

Research Group

Mascioni Alessandro, Graduate Student Researcher