Solid-State NMR Studies of Two Backbone Conformations at Tyr185 as a Function of Retinal Configurations in the Dark, Light, and Pressure Adapted Bacteriorhodopsins

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...

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Veröffentlicht in:	Journal of the American Chemical Society 2007-02, Vol.129 (5), p.1016-1017
Hauptverfasser:	Kawamura, Izuru, Kihara, Naoki, Ohmine, Masato, Nishimura, Katsuyuki, Tuzi, Satoru, Saitô, Hazime, Naito, Akira
Format:	Artikel
Sprache:	eng
Schlagworte:	Bacteriorhodopsins - chemistry Darkness Halobacterium salinarum - chemistry Isomerism Light Magnetic Resonance Spectroscopy - methods Molecular Conformation Retinaldehyde - chemistry Retinaldehyde - metabolism Stress, Mechanical Tyrosine - chemistry
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