Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Christine Hager-Braun"'
Publikováno v:
Expert Review of Proteomics. 2:745-756
Mass spectrometry has evolved as a technique suitable for the characterization of peptides and proteins beyond their linear sequence. The advantages of mass spectrometric sample analysis are high sensitivity, high mass accuracy, rapid analysis time a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ffd2d550cdfeed2bf2578d812421f751
https://doi.org/10.1586/14789450.2.5.745
https://doi.org/10.1586/14789450.2.5.745
Publikováno v:
Biochemistry. 41:1759-1766
The initial step of infection of blood cells with the human immunodeficiency virus, HIV, is the formation of a complex of the viral envelope protein gp120 and its human receptor CD4. We have examined structural features of recombinant soluble CD4 (sC
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3cad611ffc666e631268c34701aa7a69
https://doi.org/10.1021/bi011626k
https://doi.org/10.1021/bi011626k
Autor:
Hermann Katinger, Kenneth B. Tomer, John P. Moore, Norbert Schülke, James M. Binley, Leesa J. Deterding, Christine Hager-Braun, Carol E. Parker
Publikováno v:
Journal of Virology. 75:10906-10911
Matrix-assisted laser desorption ionization mass spectrometry (MALDI-MS), in combination with proteolytic protection assays, has been used to identify the functional epitope on human immunodeficiency virus envelope glycoprotein gp41 for the broadly n
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e15e949fe0fbdfd770559e3a2d1bc3ae
https://doi.org/10.1128/jvi.75.22.10906-10911.2001
https://doi.org/10.1128/jvi.75.22.10906-10911.2001
Autor:
Christine Hager-Braun, Hjalmar P. Permentier, Kristiane A. Schmidt, Jan Amesz, Sieglinde Neerken
Publikováno v:
Biochemistry. 39:7212-7220
Electron transfer in reaction center core (RCC) complexes from the green sulfur bacteria Prosthecochloris aestuarii and Chlorobium tepidum was studied by measuring flash-induced absorbance changes. The first preparation contained approximately three
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e27edc447ff35223d76a019cd9b81295
https://doi.org/10.1021/bi992861u
https://doi.org/10.1021/bi992861u
Autor:
Sieglinde Neerken, Jan Amesz, Hjalmar P. Permentier, Mette Miller, Kristiane A. Schmidt, Christine Hager-Braun, Masami Kobayashi, Machiko Akiyama
Publikováno v:
Photosynthesis Research. 64:27-39
Photosynthetically active reaction centre core (RCC) complexes were isolated from two species of green sulfur bacteria, Prosthecochloris (Ptc.) aestuarii strain 2K and Chlorobium (Chl.) tepidum, using the same isolation procedure. Both complexes cont
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::ecad0b716aee725def9e2f8a19cb91a8
https://doi.org/10.1023/a:1026515027824
https://doi.org/10.1023/a:1026515027824
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1409:87-98
Spin polarized transient EPR spectra taken at X-band (9 GHz) and K-band (24 GHz) of membrane fragments of Chlorobium tepidum and Heliobacillus mobilis are presented along with the spectra of two fractions obtained in the purification of reaction cent
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::df478249100e37f729fc5e64b02c1c66
https://doi.org/10.1016/s0005-2728(98)00152-2
https://doi.org/10.1016/s0005-2728(98)00152-2
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1365(1-2):285-293
Bacteriochlorophyll a is extracted from the reaction center complex and the Fenna-Mathews-Olson protein (FMO) of the green sulfur bacterium Chlorobium tepidum into organic solvent at different time scales. This allows the distinction of bacteriochlor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a430abd074ff4b5ad7644683a20a7eea
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1322:163-172
The reaction center (RC) core complex was isolated from the green sulfur bacterium Chlorobium tepidum and characterized by gel electrophoresis, gel filtration, and analytical ultracentrifugation. The purified complex contained the PscA and PscC subun
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a4b3a1cc0de9e4fec2c47fec70ad5279
https://doi.org/10.1016/s0005-2728(97)00073-x
https://doi.org/10.1016/s0005-2728(97)00073-x
Publikováno v:
Photosynthesis Research. 51:127-136
uttner M, Zimmermann R, Deutzmann R, Hauska G and Nelson N (1995) Biochemistry 34: 9617‐9624) were compared for the species Chlorobium limicolaand Chlorobium tepidum. In addition, membrane samples from a third green sulfur bacterium, Chlorobium vib
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::89b84ebb678935589e88f7025bd5e574
https://doi.org/10.1023/a:1005787209977
https://doi.org/10.1023/a:1005787209977
Autor:
Nikolaus Schneebauer, Nathan Nelson, Ute Feiler, Markus Fuhrmann, Günter Hauska, Christine Hager-Braun, Nicole Frankenberg, Hans Rogl
Publikováno v:
Photochemistry and Photobiology. 64:14-19
Membranes of Chlorobium tepidum contain about 35, 45 and2–10 molecules of menaquinone-7, chlorobium quinone (1′-oxo-menaquinone-7) and of the polar menaquinone (probably 1′-OH-menaquinone-7) per reaction center, respectively. None of these quin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::7bf100db0ce35d461a02ab0dc78f5f82
https://doi.org/10.1111/j.1751-1097.1996.tb02415.x
https://doi.org/10.1111/j.1751-1097.1996.tb02415.x