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Biochemistry|April 11, 1995
Effects of substitution of tyrosine 57 with asparagine and phenylalanine on the properties of bacteriorhodopsinR Govindjec, M Kono, S P Balashov, et al.Biofizika|November 1, 1976
[EPR and low temperature spectrophotometric study of the phototransformation products of bacteriorhodopsin]G T Rikhireva, M K Pulatova, S P Balashov, et al.Biophysical Journal|August 1, 1996
Arginine-82 regulates the pKa of the group responsible for the light-driven proton release in bacteriorhodopsinR Govindjee, S Misra, S P Balashov, et al.Biochemistry|August 24, 2000
Relocation of internal bound water in bacteriorhodopsin during the photoreaction of M at low temperatures: an FTIR studyA Maeda, F L Tomson, R B Gennis, et al.Biochemistry|July 22, 1997
Glutamate-194 to cysteine mutation inhibits fast light-induced proton release in bacteriorhodopsinS P Balashov, E S Imasheva, T G Ebrey, et al.Biophysical Journal|November 5, 1999
Two groups control light-induced Schiff base deprotonation and the proton affinity of Asp85 in the Arg82 his mutant of bacteriorhodopsinE S Imasheva, S P Balashov, T G Ebrey, et al.Biochemistry|March 1, 2000
Evidence for the rate of the final step in the bacteriorhodopsin photocycle being controlled by the proton release group: R134H mutantM Lu, S P Balashov, T G Ebrey, et al.Biochemistry|July 11, 1995
The two pKa's of aspartate-85 and control of thermal isomerization and proton release in the arginine-82 to lysine mutant of bacteriorhodopsinS P Balashov, R Govindjee, E S Imasheva, et al.Biochemistry|October 31, 2001
Exploring the function of Tyr83 in bacteriorhodopsin: features of the Y83F and Y83N mutantsE S Imasheva, M Lu, S P Balashov, et al.Biophysical Journal|February 1, 1997
Mutation of a surface residue, lysine-129, reverses the order of proton release and uptake in bacteriorhodopsin; guanidine hydrochloride restores itR Govindjee, E S Imasheva, S Misra, et al.Pageof 7