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Asp85 is the only internal aspartic acid that gets protonated in the M intermediate and the purple-to-blue transition of bacteriorhodopsin. A solid-state 13C CP-MAS NMR investigation

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Siebert,  Friedrich
Institut für Biophysik und Strahlenbiologie der Universität, Freiburg, Germany.;
Transport Proteins Group, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Metz, G., Siebert, F., & Engelhard, M. (1992). Asp85 is the only internal aspartic acid that gets protonated in the M intermediate and the purple-to-blue transition of bacteriorhodopsin. A solid-state 13C CP-MAS NMR investigation. FEBS Letters, 303(2-3), 237-4. doi:10.1016/0014-5793(92)80528-O.


Cite as: http://hdl.handle.net/21.11116/0000-0007-AEE3-5
Abstract
High-resolution solid-state 13C NMR spectra of the ground state and M intermediate of the bacteriorhodopsin mutant D96N with the isotope label at [4-13C]Asp and [11-13C]Trp were recorded. The NMR spectra show that Asp85 is protonated in the M intermediate. The environment of Asp85 is quite hydrophobic. On the other hand, Asp212 remains deprotonated and a slight shift to lower field indicates a more hydrophilic environment. Asp85 also protonates in the purple-to-blue transition of bacteriorhodopsin in the deionized membrane, where it experiences a similar environment to M. The shift of Trp resonances in M reflect a conformational change of the protein in forming the M intermediate.