Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Carsten Ryttersgaard"'
Autor:
Morgan Beeby, Brian D O'Connor, Carsten Ryttersgaard, Daniel R Boutz, L Jeanne Perry, Todd O Yeates
Publikováno v:
PLoS Biology, Vol 3, Iss 9, p e309 (2005)
Thermophilic organisms flourish in varied high-temperature environmental niches that are deadly to other organisms. Recently, genomic evidence has implicated a critical role for disulfide bonds in the structural stabilization of intracellular protein
Externí odkaz:
https://doaj.org/article/4278c1add0ed43ee8ef0a9ecfbef71ba
Autor:
Leila Lo Leggio, Peter Rahbek Østergaard, Jérôme Le Nours, Lars Lehmann Hylling Christensen, Carsten Ryttersgaard, Sine Larsen, Torben Vedel Borchert
Publikováno v:
Protein Science. 12:1195-1204
beta-1,4-Galactanases hydrolyze the galactan side chains that are part of the complex carbohydrate structure of the pectin. They are assigned to family 53 of the glycoside hydrolases and display significant variations in their pH and temperature opti
Autor:
Daniel R. Boutz, Carsten Ryttersgaard, Morgan Beeby, L. Jeanne Perry, Brian O'Connor, Todd O. Yeates
Publikováno v:
PLoS Biology
PLoS Biology, Vol 3, Iss 9, p e309 (2005)
PLoS Biology, Vol 3, Iss 9, p e309 (2005)
Thermophilic organisms flourish in varied high-temperature environmental niches that are deadly to other organisms. Recently, genomic evidence has implicated a critical role for disulfide bonds in the structural stabilization of intracellular protein
Autor:
Carsten Ryttersgaard, Scott C. Griffith, Duncan C. MacLaren, Todd O. Yeates, Steven Clarke, Michael R. Sawaya
Publikováno v:
The Journal of biological chemistry. 277(12)
The enzyme l-isoaspartyl methyltransferase initiates the repair of damaged proteins by recognizing and methylating isomerized and racemized aspartyl residues in aging proteins. The crystal structure of the human enzyme containing a bound S-adenosyl-l
Autor:
Carsten Ryttersgaard, Mads Eskelund Bjørnvad, Sine Larsen, A. Martin SCHüLEIN, Michael A. McDonough, Leila Lo Leggio, Sanne Schrøder Glad
Publikováno v:
University of Copenhagen
Pectate lyase is an enzyme involved in the degradation of the pectate portion of the primary plant cell wall. A recombinant pectate lyase from Thermotoga maritima where three of the four cysteine residues have been mutated (C132I, C156N, C194L) has b
Autor:
Carsten Ryttersgaard, Sine Larsen
Publikováno v:
University of Copenhagen
A disordered tartrate ion of the title compound, 2C20H25N2O2·C4H4O6·H2O, is located on the crystallographic twofold axis. Hydrogen bonds are formed between the carboxylate group and the quinuclidine group of the protonated quinine ion.
Autor:
Thomas Sandal, Sine Larsen, Jens-Christian N. Poulsen, Stephan Christgau, Henrik Dalbøge, Carsten Ryttersgaard
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 55:929-930
Recombinant β-1,4-galactanase from Aspergillus aculeatus has been crystallized and characterized by X-ray diffraction. Crystals were obtained in hanging drops by vapour-diffusion under the conditions 30% PEG 400, 0.2 M CaCl2 and 0.1 M Na HEPES buffe
Autor:
McDonough, Michael A., Carsten Ryttersgaard, Mads Eskelund Bjørnvad, Lo Leggio, Leila, Martin Schulein, Schroder Glad, Sanne O., Larsen, Sine
Publikováno v:
Acta Crystallographica: Section D (Wiley-Blackwell); Apr2002, Vol. 58 Issue 4, p709-711, 3p
Autor:
Sine Larsen, Leila Lo Leggio, Christel Thea Jørgensen, Carsten Ryttersgaard, Lars Lehmann Hylling Christensen, Mads Eskelund Bjørnvad, Jérôme Le Nours
Publikováno v:
Monash University
The beta-1,4-galactanase from Bacillus licheniformis (BLGAL) is a plant cell-wall-degrading enzyme involved in the hydrolysis of beta-1,4-galactan in the hairy regions of pectin. The crystal structure of BLGAL was determined by molecular replacement
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::07ab3e364c068a0b80e540d98e15fbca
https://research.monash.edu/en/publications/b920df71-27d3-48fa-8c18-404898866f1f
https://research.monash.edu/en/publications/b920df71-27d3-48fa-8c18-404898866f1f
Autor:
Carsten Ryttersgaard, Sine Larsen
Publikováno v:
University of Copenhagen
Two symmetry-related cinchonidinium ions of the title compound, C19H23N2O+·0.5C4H4O62−·H2O, are linked through hydrogen bonds, with a tartrate ion positioned on the twofold axis.
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4d51bf4c105f3f66b1a985701b7126e9
https://curis.ku.dk/portal/en/publications/cinchonidinium-rrtartrate-monohydrate(a7baf0a0-74c4-11db-bee9-02004c4f4f50).html
https://curis.ku.dk/portal/en/publications/cinchonidinium-rrtartrate-monohydrate(a7baf0a0-74c4-11db-bee9-02004c4f4f50).html