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

D G Nettesheim

Showing results (1-10 of 17) with videos related to

Pageof 2
Sort By:
Biochemistry|November 19, 1985
Products of metal exchange reactions of metallothioneinD G Nettesheim, H R Engeseth, J D Otvos
Biochimica Et Biophysica Acta|December 3, 1980
The role of histidine-42 in the oxidation-reduction mechanism of Chromatium vinosum high potential iron-sulfur proteinD G Nettesheim, W V Johnson, B A Feinberg
Biochemistry|February 4, 1992
Sequential resonance assignments of oxidized high-potential iron-sulfur protein from Chromatium vinosumD G Nettesheim, S R Harder, B A Feinberg, et al.
The Journal of Biological Chemistry|July 10, 1983
Comparative nuclear magnetic resonance studies of high potential iron-sulfur proteins from Chromatium vinosum and Rhodopseudomonas gelatinosa. Additional hyperfine shifted resonances and pH-dependent structural perturbationsD G Nettesheim, T E Meyer, B A Feinberg, et al.
Biochemistry|January 10, 1989
Tertiary structure of human complement component C5a in solution from nuclear magnetic resonance dataE R Zuiderweg, D G Nettesheim, K W Mollison, et al.
Experientia. Supplementum|January 1, 1987
Interprotein metal exchange reactions of metallothioneinJ D Otvos, H R Engeseth, D G Nettesheim, et al.
Proceedings of the National Academy of Sciences of the United States of America|July 1, 1988
Secondary structure of complement component C3a anaphylatoxin in solution as determined by NMR spectroscopy: differences between crystal and solution conformationsD G Nettesheim, R P Edalji, K W Mollison, et al.
Biochemistry|February 21, 1989
Proton nuclear magnetic resonance studies on the variant-3 neurotoxin from Centruroides sculpturatus Ewing: sequential assignment of resonancesD G Nettesheim, R E Klevit, G Drobny, et al.
Biochemistry|February 21, 1989
Proton nuclear magnetic resonance characterization of the aromatic residues in the variant-3 neurotoxin from Centruroides sculpturatus EwingN R Krishna, D G Nettesheim, R E Klevit, et al.
Proceedings of the National Academy of Sciences of the United States of America|November 22, 1994
The secondary structure of the ets domain of human Fli-1 resembles that of the helix-turn-helix DNA-binding motif of the Escherichia coli catabolite gene activator proteinH Liang, E T Olejniczak, X Mao, et al.
Pageof 2

Showing results (1-10 of 17) with videos related to

Sort By:
Pageof 2
Biochemistry|November 19, 1985
Products of metal exchange reactions of metallothioneinD G Nettesheim, H R Engeseth, J D Otvos
Biochimica Et Biophysica Acta|December 3, 1980
The role of histidine-42 in the oxidation-reduction mechanism of Chromatium vinosum high potential iron-sulfur proteinD G Nettesheim, W V Johnson, B A Feinberg
Biochemistry|February 4, 1992
Sequential resonance assignments of oxidized high-potential iron-sulfur protein from Chromatium vinosumD G Nettesheim, S R Harder, B A Feinberg, et al.
The Journal of Biological Chemistry|July 10, 1983
Comparative nuclear magnetic resonance studies of high potential iron-sulfur proteins from Chromatium vinosum and Rhodopseudomonas gelatinosa. Additional hyperfine shifted resonances and pH-dependent structural perturbationsD G Nettesheim, T E Meyer, B A Feinberg, et al.
Biochemistry|January 10, 1989
Tertiary structure of human complement component C5a in solution from nuclear magnetic resonance dataE R Zuiderweg, D G Nettesheim, K W Mollison, et al.
Experientia. Supplementum|January 1, 1987
Interprotein metal exchange reactions of metallothioneinJ D Otvos, H R Engeseth, D G Nettesheim, et al.
Proceedings of the National Academy of Sciences of the United States of America|July 1, 1988
Secondary structure of complement component C3a anaphylatoxin in solution as determined by NMR spectroscopy: differences between crystal and solution conformationsD G Nettesheim, R P Edalji, K W Mollison, et al.
Biochemistry|February 21, 1989
Proton nuclear magnetic resonance studies on the variant-3 neurotoxin from Centruroides sculpturatus Ewing: sequential assignment of resonancesD G Nettesheim, R E Klevit, G Drobny, et al.
Biochemistry|February 21, 1989
Proton nuclear magnetic resonance characterization of the aromatic residues in the variant-3 neurotoxin from Centruroides sculpturatus EwingN R Krishna, D G Nettesheim, R E Klevit, et al.
Proceedings of the National Academy of Sciences of the United States of America|November 22, 1994
The secondary structure of the ets domain of human Fli-1 resembles that of the helix-turn-helix DNA-binding motif of the Escherichia coli catabolite gene activator proteinH Liang, E T Olejniczak, X Mao, et al.
Pageof 2