Structural Investigation of the Active Site in Bacteriorhodopsin:  Geometric Constraints on the Roles of Asp-85 and Asp-212 in the Proton-Pumping Mechanism from Solid State NMR

Constraints on the proximity of the carboxyl carbons of the Asp-85 and Asp-212 side chains to the 14-carbon of the retinal chromophore have been established for the bR555, bR568, and M412 states of bacteriorhodopsin (bR) using solid-state NMR spectroscopy. These distances were examined via 13C−13C m...

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Veröffentlicht in:	Biochemistry (Easton) 2000-01, Vol.39 (2), p.362-371
Hauptverfasser:	Griffiths, J. M, Bennett, A. E, Engelhard, M, Siebert, F, Raap, J, Lugtenburg, J, Herzfeld, J, Griffin, R. G
Format:	Artikel
Sprache:	eng
Schlagworte:	Anisotropy Aspartic Acid - chemistry Bacteriorhodopsins - chemistry Binding Sites Magnetic Resonance Spectroscopy - methods Retinaldehyde - chemistry Spectroscopy, Fourier Transform Infrared
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