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Dynamics of the proton transfer reaction on the cytoplasmic surface of bacteriorhodopsin.
Checover S, Marantz Y, Nachliel E, Gutman M, Pfeiffer M, Tittor J, Oesterhelt D, Dencher NA. Checover S, et al. Among authors: gutman m. Biochemistry. 2001 Apr 10;40(14):4281-92. doi: 10.1021/bi002574m. Biochemistry. 2001. PMID: 11284684
The cytoplasmic surface of bacteriorhodopsin is characterized by a group of carboxylates that function as a proton attractive domain [Checover, S., Nachliel, E., Dencher, N. A., and Gutman, M. (1997) Biochemistry 36, 13919-13928]. To identify these carboxylates, we …
The cytoplasmic surface of bacteriorhodopsin is characterized by a group of carboxylates that function as a proton attractive domain [Checov …
Subsecond proton-hole propagation in bacteriorhodopsin.
Schätzler B, Dencher NA, Tittor J, Oesterhelt D, Yaniv-Checover S, Nachliel E, Gutman M. Schätzler B, et al. Among authors: gutman m. Biophys J. 2003 Jan;84(1):671-86. doi: 10.1016/S0006-3495(03)74887-5. Biophys J. 2003. PMID: 12524320 Free PMC article.
Proton transfer dynamics on the surface of the late M state of bacteriorhodopsin.
Nachliel E, Gutman M, Tittor J, Oesterhelt D. Nachliel E, et al. Among authors: gutman m. Biophys J. 2002 Jul;83(1):416-26. doi: 10.1016/S0006-3495(02)75179-5. Biophys J. 2002. PMID: 12080130 Free PMC article.
Systematic replacement of most of the surface carboxylates indicated that the cluster is made of D104, E161, and E234 (Checover, S., Y. Marantz, E. Nachliel, M. Gutman, M. Pfeiffer, J. Tittor, D. Oesterhelt, and N. Dencher. 2001. ...The triple mutant resemble …
Systematic replacement of most of the surface carboxylates indicated that the cluster is made of D104, E161, and E234 (Checover, S., Y. Mara …
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