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Hydrogen bonding interactions with the Schiff base of bacteriorhodopsin. Resonance Raman spectroscopy of the mutants D85N and D85A.
Rath P, Marti T, Sonar S, Khorana HG, Rothschild KJ. Rath P, et al. Among authors: marti t. J Biol Chem. 1993 Aug 25;268(24):17742-9. J Biol Chem. 1993. PMID: 8349659 Free article.
The bacteriorhodopsin (bR) mutants Asp-85-->Asn (D85N) and Asp-85-->Ala (D85A) have a red-shifted chromophore absorption and exhibit no proton pumping (Otto, H., Marti, T., Holz, M., Mogi, T., Stern, L., Engel, F., Khorana, H. ...U.S.A. 87, 1018-1022) c …
The bacteriorhodopsin (bR) mutants Asp-85-->Asn (D85N) and Asp-85-->Ala (D85A) have a red-shifted chromophore absorption and exhibit n …
Anion binding to the Schiff base of the bacteriorhodopsin mutants Asp-85----Asn/Asp-212----Asn and Arg-82----Gln/Asp-85----Asn/Asp-212----Asn.
Marti T, Otto H, Rösselet SJ, Heyn MP, Khorana HG. Marti T, et al. J Biol Chem. 1992 Aug 25;267(24):16922-7. J Biol Chem. 1992. PMID: 1512233 Free article.
Studies of bacteriorhodopsin have indicated that the charge environment of the protonated Schiff base consists of residues Asp-85, Asp-212, and Arg-82. As shown recently (Marti, T., Rosselet, S. J., Otto, H., Heyn, M. P., and Khorana, H. ...
Studies of bacteriorhodopsin have indicated that the charge environment of the protonated Schiff base consists of residues Asp-85, Asp-212, …
282 results