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Your search keyword '"Site-directed 13C solid-state NMR"' showing total 2 results
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2 results on '"Site-directed 13C solid-state NMR"'

1. Dynamic structure of pharaonis phoborhodopsin (sensory rhodopsin II) and complex with a cognate truncated transducer as revealed by site-directed 13C solid-state NMR

Author

Arakawa, Tadashi, Shimono, Kazumi, Yamaguchi, Satoru, Tuzi, Satoru, Sudo, Yuki, Kamo, Naoki, and Saitô, Hazime

Subjects
*RHODOPSIN, *NUCLEAR magnetic resonance spectroscopy
Abstract

We have recorded 13C nuclear magnetic resonance (NMR) spectra of [3-13C]Ala, [1-13C]Val-labeled pharaonis phoborhodopsin (ppR or sensory rhodopsin II) incorporated into egg PC (phosphatidylcholine) bilayer, by means of site-directed high-resolution solid-state NMR techniques. Seven 13C NMR signals from transmembrane α-helices were resolved for [3-13C]Ala-ppR at almost the same positions as those of bacteriorhodopsin (bR), except for the suppressed peaks in the loop regions in spite of the presence of at least three Ala residues. In contrast, 13C NMR signals from the loops were visible from [1-13C]Val-ppR but their peak positions of the transmembrane α-helices are not always the same between ppR and bR. The motional frequency of the loop regions in ppR was estimated as 105 Hz in view of the suppressed peaks from [3-13C]Ala-ppR due to interference with proton decoupling frequency. We found that conformation and dynamics of ppR were appreciably altered by complex formation with a cognate truncated transducer pHtr II (1–159). In particular, the C-terminal α-helix protruding from the membrane surface is involved in the complex formation and subsequent fluctuation frequency is reduced by one order of magnitude. [Copyright &y& Elsevier]

Published
2003
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2. Dynamic structure of pharaonis phoborhodopsin (sensory rhodopsin II) and complex with a cognate truncated transducer as revealed by site-directed 13 C solid-state NMR

Author

Kazumi Shimono, Satoru Tuzi, Tadashi Arakawa, Naoki Kamo, Satoru Yamaguchi, Hazime Saitô, and Yuki Sudo

Subjects
Site-directed 13C solid-state NMR, Macromolecular Substances, Protein Conformation, Archaeal Proteins, Lipid Bilayers, Biophysics, Biochemistry, chemistry.chemical_compound, Conformation and dynamics, Protein structure, Nuclear magnetic resonance, Cognate transducer, Structural Biology, Phosphatidylcholine, Genetics, Sensory Rhodopsins, Nuclear Magnetic Resonance, Biomolecular, Molecular Biology, Sensory rhodopsin II, Carbon Isotopes, biology, Bilayer, Bacteriorhodopsin, Cell Biology, Carbon-13 NMR, Pharaonis phoborhodopsin, Carotenoids, Transmembrane protein, Crystallography, chemistry, Solid-state nuclear magnetic resonance, Membrane protein, Bacteriorhodopsins, Mutagenesis, Site-Directed, Phosphatidylcholines, biology.protein, Halorhodopsins, Signal Transduction
Abstract

We have recorded (13)C nuclear magnetic resonance (NMR) spectra of [3-(13)C]Ala, [1-(13)C]Val-labeled pharaonis phoborhodopsin (ppR or sensory rhodopsin II) incorporated into egg PC (phosphatidylcholine) bilayer, by means of site-directed high-resolution solid-state NMR techniques. Seven (13)C NMR signals from transmembrane alpha-helices were resolved for [3-(13)C]Ala-ppR at almost the same positions as those of bacteriorhodopsin (bR), except for the suppressed peaks in the loop regions in spite of the presence of at least three Ala residues. In contrast, (13)C NMR signals from the loops were visible from [1-(13)C]Val-ppR but their peak positions of the transmembrane alpha-helices are not always the same between ppR and bR. The motional frequency of the loop regions in ppR was estimated as 10(5) Hz in view of the suppressed peaks from [3-(13)C]Ala-ppR due to interference with proton decoupling frequency. We found that conformation and dynamics of ppR were appreciably altered by complex formation with a cognate truncated transducer pHtr II (1-159). In particular, the C-terminal alpha-helix protruding from the membrane surface is involved in the complex formation and subsequent fluctuation frequency is reduced by one order of magnitude.

Published
2003
Full Text
View/download PDF

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