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Biophysical Journal|March 1, 1992
A residue substitution near the beta-ionone ring of the retinal affects the M substates of bacteriorhodopsinG Váró, L Zimányi, M Chang, et al.FEBS Letters|October 25, 1993
Trimeric mutant bacteriorhodopsin, D85N, shows a monophasic CD spectrumM Kataoka, K Mihara, H Kamikubo, et al.Biochemistry|November 12, 1991
Water is required for proton transfer from aspartate-96 to the bacteriorhodopsin Schiff baseY Cao, G Váró, M Chang, et al.Biochemistry|July 22, 1999
Existence of two L photointermediates of halorhodopsin from Halobacterium salinarium, differing in their protein and water FTIR bandsY S Chon, H Kandori, J Sasaki, et al.Biophysical Journal|April 1, 1995
Relationship of proton release at the extracellular surface to deprotonation of the schiff base in the bacteriorhodopsin photocycleY Cao, L S Brown, J Sasaki, et al.Journal of Molecular Biology|June 10, 1994
The proton transfers in the cytoplasmic domain of bacteriorhodopsin are facilitated by a cluster of interacting residuesL S Brown, Y Yamazaki, A Maeda, et al.Biochemistry|March 1, 1994
A covalent link between the chromophore and the protein backbone of bacteriorhodopsin is not required for forming a photochemically active pigment analogous to the wild typeN Friedman, S Druckmann, J Lanyi, et al.The Journal of Biological Chemistry|November 10, 1995
Glutamic acid 204 is the terminal proton release group at the extracellular surface of bacteriorhodopsinL S Brown, J Sasaki, H Kandori, et al.Journal of Biochemistry|February 28, 2001
Surface dynamics of bacteriorhodopsin as revealed by (13)C NMR studies on [(13)C]Ala-labeled proteins: detection of millisecond or microsecond motions in interhelical loops and C-terminal alpha-helixS Yamaguchi, S Tuzi, K Yonebayashi, et al.Proceedings of the National Academy of Sciences of the United States of America|February 20, 1996
Structure of the N intermediate of bacteriorhodopsin revealed by x-ray diffractionH Kamikubo, M Kataoka, G Váró, et al.Pageof 9