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Kühlbrandt (P1) | Dötsch/Bernhard (P2) | Michel (P3) | Ziegler (P4) | Mäntele (P5) | Glaubitz (P6) | Forrest (P8) | Fendler/Bamberg (P10)

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Secondary transporters convert the free energy stored in electrochemical gradients into a substrate concentration gradient. This process takes place using substrate/ion antiport or symport. Although close to ten X-ray structures, including contributions from Frankfurt, have been determined, a detailed understanding of a universal structure-function relationship has not been achieved so far. Therefore, a proteome-wide approach as well as in-depth molecular studies on selected proteins is proposed.

A proteome-wide analysis of transporters from E. coli and of selected transporter families from Aquifex aeolicus, Salmonella typhimurium, Pyrococcus furiosus and Homo sapiens will be carried out. A systematic screen of expression conditions using cell-free expression systems aims at finding suitable candidates for further structural and functional analyses. In a collaborative effort these proteins will be further characterized by electron paramagnetic resonance, FTIR spectroscopy, and electrophysiology.

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