Scientists from the Max Planck Institute of Biochemistry in Martinsried, Germany, and the Institute of Structural Biology in Grenoble, France, used neutron beams to expand current knowledge on structure-function relations in the ion pump bacteriorhodopsin. By using isotope-labeled membranes, areas of different dynamical behavior were detected, and a functionally essential Glycolipid was localized.
A collaboration between biochemists Heiko Patzelt and Dieter Oesterhelt from Munich's Max Planck Institute of Biochemistry and biophysicists Martin Weik, Valrie Rat and Giuseppe Zaccai from the Institute of Structural Biology in Grenoble yielded new and unusual insights into the structure-function relations in the light-driven proton pump bacteriorhodopsin. Using neutron spectroscopy and diffraction experiments, which are sensitive to isotope labels, areas of differential dynamical behavior within the protein, as well as the position of functionally important lipids surrounding it, were localized. The discoveries were recently published in Molecular Cell (1998, vol. 1, 411-419) and in the Proceedings of the National Academy of Science of the USA (1998, vol. 49, 4970-4975).
Membrane proteins play key roles in the functioning of the living cell. Apart from very few
exceptions, their structure-function relations, however, still remain unclear. The light-driven
proton pump bacteriorhodopsin, the photosynthetic retinal-protein in the cell walls of the
salt-loving microorganism Halobacterium salinarum, can be prepared in selectively
isotope-labeled forms. In addition to neutron diffraction (Journal of Molecular Biology 1989,
210, 829-847) and Nuclear Magnetic Resonance (NMR) investigations (Journal of
Contact: Dieter Oesterhelt