Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Filters

M P Heyn

Showing results (51-60 of 64) with videos related to

Pageof 7
Sort By:
Biochemistry|November 30, 1993
X-ray diffraction of a cysteine-containing bacteriorhodopsin mutant and its mercury derivative. Localization of an amino acid residue in the loop of an integral membrane proteinM P Krebs, W Behrens, R Mollaaghababa, et al.
Proceedings of the National Academy of Sciences of the United States of America|February 15, 1992
Consequences of amino acid insertions and/or deletions in transmembrane helix C of bacteriorhodopsinT Marti, H Otto, S J Rösselet, et al.
The Journal of Biological Chemistry|October 5, 1991
The retinylidene Schiff base counterion in bacteriorhodopsinT Marti, S J Rösselet, H Otto, et al.
Biochemistry|October 8, 1999
The angles between the C(1)-, C(5)-, and C(9)-methyl bonds of the retinylidene chromophore and the membrane normal increase in the M intermediate of bacteriorhodopsin: direct determination with solid-state (2)H NMRS Moltke, I Wallat, N Sakai, et al.
Proceedings of the National Academy of Sciences of the United States of America|February 1, 1991
Expression of the bacterioopsin gene in Halobacterium halobium using a multicopy plasmidM P Krebs, T Hauss, M P Heyn, et al.
The Journal of Biological Chemistry|December 25, 1992
Effect of introducing different carboxylate-containing side chains at position 85 on chromophore formation and proton transport in bacteriorhodopsinD A Greenhalgh, S Subramaniam, U Alexiev, et al.
The Journal of Biological Chemistry|April 15, 1991
Bacteriorhodopsin mutants containing single substitutions of serine or threonine residues are all active in proton translocationT Marti, H Otto, T Mogi, et al.
Proceedings of the National Academy of Sciences of the United States of America|December 1, 1989
Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsinH Otto, T Marti, M Holz, et al.
Proceedings of the National Academy of Sciences of the United States of America|December 5, 1995
Proton transport by a bacteriorhodopsin mutant, aspartic acid-85-->asparagine, initiated in the unprotonated Schiff base stateS Dickopf, U Alexiev, M P Krebs, et al.
Proceedings of the National Academy of Sciences of the United States of America|February 1, 1990
Substitution of amino acids Asp-85, Asp-212, and Arg-82 in bacteriorhodopsin affects the proton release phase of the pump and the pK of the Schiff baseH Otto, T Marti, M Holz, et al.
Pageof 7

Showing results (51-60 of 64) with videos related to

Sort By:
Pageof 7
Biochemistry|November 30, 1993
X-ray diffraction of a cysteine-containing bacteriorhodopsin mutant and its mercury derivative. Localization of an amino acid residue in the loop of an integral membrane proteinM P Krebs, W Behrens, R Mollaaghababa, et al.
Proceedings of the National Academy of Sciences of the United States of America|February 15, 1992
Consequences of amino acid insertions and/or deletions in transmembrane helix C of bacteriorhodopsinT Marti, H Otto, S J Rösselet, et al.
The Journal of Biological Chemistry|October 5, 1991
The retinylidene Schiff base counterion in bacteriorhodopsinT Marti, S J Rösselet, H Otto, et al.
Biochemistry|October 8, 1999
The angles between the C(1)-, C(5)-, and C(9)-methyl bonds of the retinylidene chromophore and the membrane normal increase in the M intermediate of bacteriorhodopsin: direct determination with solid-state (2)H NMRS Moltke, I Wallat, N Sakai, et al.
Proceedings of the National Academy of Sciences of the United States of America|February 1, 1991
Expression of the bacterioopsin gene in Halobacterium halobium using a multicopy plasmidM P Krebs, T Hauss, M P Heyn, et al.
The Journal of Biological Chemistry|December 25, 1992
Effect of introducing different carboxylate-containing side chains at position 85 on chromophore formation and proton transport in bacteriorhodopsinD A Greenhalgh, S Subramaniam, U Alexiev, et al.
The Journal of Biological Chemistry|April 15, 1991
Bacteriorhodopsin mutants containing single substitutions of serine or threonine residues are all active in proton translocationT Marti, H Otto, T Mogi, et al.
Proceedings of the National Academy of Sciences of the United States of America|December 1, 1989
Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsinH Otto, T Marti, M Holz, et al.
Proceedings of the National Academy of Sciences of the United States of America|December 5, 1995
Proton transport by a bacteriorhodopsin mutant, aspartic acid-85-->asparagine, initiated in the unprotonated Schiff base stateS Dickopf, U Alexiev, M P Krebs, et al.
Proceedings of the National Academy of Sciences of the United States of America|February 1, 1990
Substitution of amino acids Asp-85, Asp-212, and Arg-82 in bacteriorhodopsin affects the proton release phase of the pump and the pK of the Schiff baseH Otto, T Marti, M Holz, et al.
Pageof 7