Solid-State NMR Studies of Two Backbone Conformations at Tyr185 as a Function of Retinal Configurations in the Dark, Light, and Pressure Adapted Bacteriorhodopsins
| العنوان: | Solid-State NMR Studies of Two Backbone Conformations at Tyr185 as a Function of Retinal Configurations in the Dark, Light, and Pressure Adapted Bacteriorhodopsins |
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| المؤلفون: | Katsuyuki Nishimura, Masato Ohmine, Satoru Tuzi, Akira Naito, Izuru Kawamura, Naoki Kihara, Hazime Saitô |
| المصدر: | Journal of the American Chemical Society. 129:1016-1017 |
| بيانات النشر: | American Chemical Society (ACS), 2007. |
| سنة النشر: | 2007 |
| مصطلحات موضوعية: | Halobacterium salinarum, Magnetic Resonance Spectroscopy, Light, Molecular Conformation, Biochemistry, Catalysis, Spectral line, chemistry.chemical_compound, Colloid and Surface Chemistry, Nuclear magnetic resonance, Isomerism, Singlet state, biology, Resonance, Retinal, Bacteriorhodopsin, General Chemistry, Darkness, Carbon-13 NMR, Crystallography, chemistry, Solid-state nuclear magnetic resonance, Bacteriorhodopsins, Retinaldehyde, biology.protein, Tyrosine, Stress, Mechanical |
| الوصف: | Backbone conformations near tyrosine in bacteriorhodopsin (bR) corresponding to all-trans and 13-cis retinal configurations in the dark, light, and pressure adapted states were investigated for Tyr-X peptide bonds by using double amino acid labeling with [1-13C]Tyr, [15N]X-bR by means of rotational echo double resonance (REDOR) technique. The NMR signals obtained from the difference spectra between REDOR and full echo experiments allowed selectively detect on a tyrosine signals for Tyr185-Pro186, Tyr26-Phe27, and Tyr64-Gly65. Two 13C NMR peaks were observed for REDOR-filtered spectrum of Tyr185 in the dark at ambient temperature. These two signals are attributed to the bR with all-trans and 13-cis retinals. REDOR-filtered spectra for Tyr26 and 64 show singlet lines because they are located far from the retinal. All-trans peak intensity was increased in the light adapted state, while the 13-cis state increased for the pressure-adapted state. These results indicate that REDOR-filtered experiments provide us... |
| تدمد: | 1520-5126 0002-7863 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f9bcc04a1a048d6066931cc6820d9f79 https://doi.org/10.1021/ja0664887 |
| رقم الأكسشن: | edsair.doi.dedup.....f9bcc04a1a048d6066931cc6820d9f79 |
| قاعدة البيانات: | OpenAIRE |
Find this issue from the American Chemical Society | تدمد: | 15205126 00027863 |
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