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Very Fruitful Collaboration Between French And German Scientists Yields Unusual Insights Into The Structure Of Membrane Proteins

Biomolecular NMR 1997, 10, 95-106), this now allowed the use of neutron spectroscopy to address specific dynamics which has, for the first time, been tackled in a membrane protein. The experiments were performed at the High-Flux Neutron Reactor of the Institut von Laue-Langevin in Grenoble.

Elastic incoherent neutron scattering (EINS) experiments on selectively deuterated bacteriorhodopsin, which make it possible to define amplitudes of thermal motions in the nano- to picosecond time-scale, have revealed a dynamic transition from a harmonic to a softer, inharmonic atomic fluctuation regime in the global behavior of the protein. Biological activity in proteins is correlated with this transition, suggesting that this type of flexibility is a prerequisite for function. The thermal motions of the labeled atoms in the heart of the protein, however, demonstrate stiffer behavior and, at room temperature, they have significantly smaller amplitudes of motion. Contrary to the bulk mean behavior, they appear to be shielded from solvent melting effects. These experimental results quantify the dynamical heterogeneity of bacteriorhodopsin, which meets the functional requirements of bulk flexibility, on the one hand, to allow large conformational changes in the molecule, and of a harder core, on the other, to control stereo-specific conformation changes of the central retinal.

It was shown here that protein atoms move in potential wells of different shapes and temperature characteristics, depending on their location in the structure. The EINS experiments have proven to be sufficiently sensitive to quantify this dynamical heterogeneity. The neutron approach yields the most direct and possibly unique qua
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Contact: Dieter Oesterhelt
oesterhe@biochem.mpg.de
+49-89-8578-2386
Max-Planck-Gesellschaft
14-May-1998


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