S P Balashov - JoVE Visualize

Showing results (21-30 of 31) with videos related to

Pageof 4

Sort By:

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.

Biochemistry|October 5, 1993

Effect of the arginine-82 to alanine mutation in bacteriorhodopsin on dark adaptation, proton release, and the photochemical cycleS P Balashov, R Govindjee, M Kono, et al.

Biochemistry|February 23, 1999

The proton release group of bacteriorhodopsin controls the rate of the final step of its photocycle at low pHS P Balashov, M Lu, E S Imasheva, et al.

Biochemistry|June 29, 2012

Aspartate-histidine interaction in the retinal schiff base counterion of the light-driven proton pump of Exiguobacterium sibiricumS P Balashov, L E Petrovskaya, E P Lukashev, et al.

Pageof 4

Showing results (21-30 of 31) with videos related to

Sort By:

Pageof 4

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.

Biochemistry|October 5, 1993

Effect of the arginine-82 to alanine mutation in bacteriorhodopsin on dark adaptation, proton release, and the photochemical cycleS P Balashov, R Govindjee, M Kono, et al.

Biochemistry|February 23, 1999

The proton release group of bacteriorhodopsin controls the rate of the final step of its photocycle at low pHS P Balashov, M Lu, E S Imasheva, et al.

Biochemistry|June 29, 2012

Aspartate-histidine interaction in the retinal schiff base counterion of the light-driven proton pump of Exiguobacterium sibiricumS P Balashov, L E Petrovskaya, E P Lukashev, et al.

Pageof 4