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High-resolution solid state carbon-13C NMR of bacteriorhodopsin: characterization of [4-13C]Asp resonances

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Siebert,  Friedrich
Institut für Biophysik und Strahlenbiologie der Universität Freiburg, 7800 Freiburg, Germany;
Transport Proteins Group, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Metz, G., Siebert, F., & Englehard, M. (1992). High-resolution solid state carbon-13C NMR of bacteriorhodopsin: characterization of [4-13C]Asp resonances. Biochemistry, 31(2), 455-462. doi:10.1021/bi00117a022.


Cite as: http://hdl.handle.net/21.11116/0000-0007-AEEB-D
Abstract
Solid state 13C nuclear magnetic resonance measurements of bacteriorhodopsin labeled with [4-13C]Asp show that resonances of single amino acids can be resolved. In order to assign and characterize the resonances of specific Asp residues, three different approaches were used. (1) Determination of the chemical shift anisotropy from side-band intensities provides information about the protonation state of Asp residues. (2) Relaxation studies and T1 filtering allow one to discriminate between resonances with different mobility. (3) A comparison of the spectra of light- and dark-adapted bacteriorhodopsin provides evidence for resonances from aspartic acid residues in close neighborhood of the chromophore. In agreement with other investigations, four resonances are assigned to internal residues. Two of them are protonated in the ground state up to pH 10 (Asp96 and Asp115). All other detected resonances, including Asp85 and Asp212, are due to deprotonated aspartic acid. Two lines due to the two internal deprotonated groups change upon dark and light adaptation, whereas the protonated Asp residues are unaffected.