The biochemistry research teams at CMB constitutes a world-leading research environment for membrane protein structural biology that aims at deepening our understanding of membrane protein structure-function relationships in the cellular environment, and at developing new and innovative methods for production and characterization of membrane proteins.
Membrane proteins govern energy transduction, control cellular ion and metabolite concentrations, interpret the cellular environment and initiate responses to external stimuli. A high-resolution structure of a membrane protein provides unique insight into how it performs remarkable chemical processes within the cell.
Membrane protein structural biology has had major impact within the life sciences, recognized by Noble Prizes in Chemistry in 1988, 1997 and 2003. Membrane proteins also encompass the largest families of pharmaceutical targets, representing a multi-billion euro industry with tremendously positive influence on human health. Membrane proteins are dramatically underrepresented structurally (approximately 1.5 % of unique structures in the protein data bank correspond to membrane proteins) and there is an even greater paucity of structural information regarding how they change conformation during their functional cycles.
The Biophysics research constellation develops novel NMR methodologies for proteins requiring spectra of very high dimensionality and/or fast acquisition. Typical applications include structural studies of natively unfolded proteins or proteins of limited stability. Spectra with four or more dimensions are recorded using novel sampling techniques (‘projection spectroscopy’) and analyzed with adapted data decomposition algorithms (‘multi-way decomposition’). The biophysics cluster also applies EPR spectroscopy to study biological systems. This technique is used to probe molecules with unpaired electrons such as transition-metal-containing proteins and organic radicals. Electron-transfer reactions in photosynthesis and water-transport studies of aquaporins are also studied using spectroscopic tools.