Zobrazeno 1 - 10
of 174
pro vyhledávání: '"Heinz Rüterjans"'
Autor:
Marc-Michael Blum, Stephen J. Tomanicek, Paul Langan, Benno P. Schoenborn, Heinz Rüterjans, Julian C.-H. Chen, Harald John, B. Leif Hanson
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 66:379-385
The signal-to-noise ratio is one of the limiting factors in neutron macromolecular crystallography. Protein perdeuteration, which replaces all H atoms with deuterium, is a method of improving the signal-to-noise ratio of neutron crystallography exper
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::021f8483110a38c9157270572f311a59
https://doi.org/10.1107/s1744309110004318
https://doi.org/10.1107/s1744309110004318
Autor:
Paul Langan, Benno P. Schoenborn, Heinz Rüterjans, Marat Mustyakimov, Marc-Michael Blum, Kai Kehe, Julian C.-H. Chen
Publikováno v:
Proceedings of the National Academy of Sciences. 106:713-718
Hydrogen atoms constitute about half of all atoms in proteins and play a critical role in enzyme mechanisms and macromolecular and solvent structure. Hydrogen atom positions can readily be determined by neutron diffraction, and as such, neutron diffr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7a17b68b8aeadbae5c6b0a0a6eecdfda
https://doi.org/10.1073/pnas.0807842106
https://doi.org/10.1073/pnas.0807842106
Autor:
Julian C.-H. Chen, Benno P. Schoenborn, Paul Langan, Heinz Rüterjans, Marc-Michael Blum, Alexander Koglin
Publikováno v:
Acta Crystallographica Section F Structural Biology and Crystallization Communications. 63:42-45
The enzyme diisopropyl fluorophosphatase (DFPase) from Loligo vulgaris is capable of decontaminating a wide variety of toxic organophosphorus nerve agents. DFPase is structurally related to a number of enzymes, such as the medically important paraoxo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::318cb51ab40b1099699f832c3977db5a
https://doi.org/10.1107/s1744309106052924
https://doi.org/10.1107/s1744309106052924
Autor:
Bernd Ludwig, Christian Lücke, Primoz Pristovsek, Oliver Maneg, Marco D. Mukrasch, Lucia Muresanu, Heinz Rüterjans, Frank Löhr
Publikováno v:
Journal of Biological Chemistry. 281:14503-14513
The structural analysis of the redox complex between the soluble cytochrome c552 and the membrane-integral cytochrome ba3 oxidase of Thermus thermophilus is complicated by the transient nature of this protein-protein interaction. Using NMR-based chem
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::bff0d0f163b962191d50ee0f3b444026
https://doi.org/10.1074/jbc.m601108200
https://doi.org/10.1074/jbc.m601108200
Publikováno v:
ChemBioChem. 5:1523-1534
Hydrogen bonding plays a key role in the tight binding of the FMN cofactor and the regulation of its redox properties in flavodoxins. Hydrogen bonding interactions can be directly observed in solution by multidimensional heteronuclear NMR spectroscop
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::09c35affca265eb8a179b00cde5d5190
https://doi.org/10.1002/cbic.200400171
https://doi.org/10.1002/cbic.200400171
Autor:
Bhalchandra Shripad Lele, Glenn D. Papworth, Alan J. Russell, Vicky Katsemi, Igor Martyano, Kenneth J. Klabunde, Heinz Rüterjans
Publikováno v:
Biotechnology and Bioengineering. 86:628-636
We demonstrate two novel approaches to enhance interactions of polymer-immobilized biomolecules with their substrates. In the first approach, diisopropylfluorophosphatase (DFPase) containing poly(urethane) (PU) coatings were made microporous by incor
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::91f080434fe46eeb4a9c5f390b41889b
https://doi.org/10.1002/bit.20106
https://doi.org/10.1002/bit.20106
Publikováno v:
Biochemistry. 43:5820-5831
Xylanase from Bacillus agaradhaerens belongs to a large group of glycosyl hydrolases which catalyze the degradation of xylan. The protonation behavior of titratable groups of the uniformly (15)N- and (13)C-labeled xylanase was investigated by multinu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1decc52c1dcf7baf53bfedaab36f3adc
https://doi.org/10.1021/bi049948m
https://doi.org/10.1021/bi049948m
Publikováno v:
Magnetic Resonance in Chemistry. 42:321-328
Side-chain proton and carbon-13 resonance assignments of [13C;15N]-enriched proteins usually rely on combinations of several multi-dimensional experiments. Here, we describe a four-dimensional pulse sequence, H(C)C–COSY–TOCSY–(CACO)NH, which pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6dd3830a7cdef385c1971c0f9df8b142
https://doi.org/10.1002/mrc.1346
https://doi.org/10.1002/mrc.1346
Autor:
Winfried Haase, Birgit Schäfer, Heinz Rüterjans, Frank Bernhard, Clemens Glaubitz, Frank Löhr, Christian Klammt, Volker Dötsch
Publikováno v:
European Journal of Biochemistry. 271:568-580
We demonstrate the high level expression of integral membrane proteins (IMPs) in a cell-free coupled transcription/translation system using a modified Escherichia coli S30 extract preparation and an optimized protocol. The expression of the E. coli s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8c77b93e91f7f0f41bae38190fcf0cf7
https://doi.org/10.1111/j.1432-1033.2003.03959.x
https://doi.org/10.1111/j.1432-1033.2003.03959.x
Autor:
Frank Löhr, Lucia Muresanu, Ioana Kleinhaus, Primož Pristovšek, Christian Lücke, Karla Werner, Hans Wienk, Vladimir V. Rogov, Heinz Rüterjans
Publikováno v:
European Journal of Biochemistry. 270:4846-4858
Heteronuclear high-resolution NMR spectroscopy was employed to determine the solution structure of the excisionase protein (Xis) from the λ-like bacteriophage HK022 and to study its sequence-specific DNA interaction. As wild-type Xis was previously
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e7fa289a7ce373b8c92660de32cbde20
https://doi.org/10.1111/j.1432-1033.2003.03884.x
https://doi.org/10.1111/j.1432-1033.2003.03884.x