Zobrazeno 1 - 10
of 44
pro vyhledávání: '"Kim Kusk Mortensen"'
Autor:
Louise Carøe Vohlander Rasmussen, Janni M Jensen, Jan Skov Pedersen, Hans Uffe Sperling-Petersen, Cristiano L. P. Oliveira, Olwyn Byron, Kim Kusk Mortensen
Publikováno v:
Rasmussen, L C V, Oliveira, C L P, Byron, O, Jensen, J M, Pedersen, J S, Sperling-Petersen, H U & Mortensen, K K 2011, ' Structure and dimerization of translation initiation factor aIF5B in solution ', Biochemical and Biophysical Research Communications, vol. 416, pp. 140-145 . https://doi.org/10.1016/j.bbrc.2011.11.012
Translation initiation factor 5B (IF5B) is required for initiation of protein synthesis. The solution structure of archaeal IF5B (aIF5B) was analysed by small-angle X-ray scattering (SAXS) and dynamic light scattering (DLS) and was indicated to be in
Autor:
Elena I. Deryugina, Peter A. Andreasen, Kenneth A. Botkjaer, Janni M Jensen, James P. Quigley, Aleksandra A. Byszuk, Kim Kusk Mortensen, Grant E. Blouse
Publikováno v:
Journal of Biological Chemistry. 284:4647-4657
Serine proteases are secreted from cells as single-chain zymogens, typically having activities orders of magnitude lower than those of the mature two-chain enzymes. Activation occurs by a conformational change initiated by cleavage of a specific pept
Autor:
Jesper Givskov Sørensen, Kim Kusk Mortensen, Troels Skrydstrup, Janni Egebjerg, Birgit Schiøtt, Jan Pedersen, Brian Schou Rasmussen
Publikováno v:
Rasmussen, B S, Pedersen, J M, Sørensen, J, Egebjerg, J, Schiøtt, B, Mortensen, K K & Skrydstrup, T 2007, ' Enantioselective Proteins: Selection, Binding Studies and Molecular Modeling of Antibodies with Affinity towards Hydrophobic BINOL Derivatives ', ChemBioChem, vol. 8, no. 16, pp. 1974-1980 . https://doi.org/10.1002/cbic.200700295
In this paper, the initial steps towards the design of novel artificial metalloenzymes that exploit proteins as a second coordination sphere for traditional metal-ligand catalysis are described. Phage display was employed to select and study antibody
Autor:
Hans Uffe Sperling-Petersen, Kim Kusk Mortensen, Janni Egebjerg Kristensen, Hans Peter Sørensen
Publikováno v:
Sørensen, H P, Kristensen, J E, Sperling-Petersen, H U & Mortensen, K K 2004, ' Soluble expression of aggregating proteins by covalent coupling to the ribosome ', Biochemical and Biophysical Research Communications, vol. 319, no. 3, pp. 715-9 . https://doi.org/10.1016/j.bbrc.2004.05.081
Udgivelsesdato: 2004-Jul-2 Ribosomes are extremely soluble ribonucleoprotein complexes. Heterologous target proteins were fused to ribosomal protein L23 (rpL23) and expressed in an rpL23 deficient Escherichia coli strain. This enabled the isolation o
Autor:
Brian Søgaard Laursen, Anne Cecillie Kjærgaard, Hans Uffe Sperling-Petersen, Kim Kusk Mortensen, David W. Hoffman
Publikováno v:
Protein Science. 13:230-239
Bacterial translation initiation factor IF2 is a multidomain protein that is an essential component of a system for ensuring that protein synthesis begins at the correct codon within a messenger RNA. Full-length IF2 from Escherichia coli and seven fr
Publikováno v:
Extremophiles. 7:423-431
The present work reports for the first time the purification and characterisation of two extremely halotolerant endo-xylanases from a novel halophilic bacterium, strain CL8. Purification of the two xylanases, Xyl 1 and 2, was achieved by anion exchan
Publikováno v:
Journal of Biological Chemistry. 278:16320-16328
The 18-kDa Domain I from the N-terminal region of translation initiation factor IF2 from Escherichia coli was expressed, purified, and structurally characterized using multidimensional NMR methods. Residues 2-50 were found to form a compact subdomain
Publikováno v:
Enzyme and Microbial Technology. 32:721-727
Medium optimisation for a novel halophilic eubacterium, strain SX15, resulted in a 20-fold increase of extracellular xylanase activity. This facilitates the purification of xylanase produced by this strain. Prior experiments revealed that xylan conce
Autor:
Brian Søgaard Laursen, Igor Siwanowicz, Guilhem Larigauderie, John M. Kenney, Koreaki Ito, Yoshikazu Nakamura, Kim Kusk Mortensen, Hans Uffe Sperling-Petersen, Jakob Hedegaard
Publikováno v:
Laursen, B S, Siwanowicz, I, Larigauderie, G, Hedegaard, J, Ito, K, Nakamura, Y, Kenney, J M, Mortensen, K K & Sperling-Petersen, H U 2003, ' Characterization of mutations in the GTP-binding domain of IF2 resulting in cold-sensitive growth of Escherichia coli ', J. Mol. Biol., vol. 326, pp. 543-551 .
Laursen, B S, Siwanowicz, I, Larigauderie, G, Hedegaard, J, Ito, K, Nakamura, Y, Kenney, J M, Mortensen, K K & Sperling-Petersen, H U 2003, ' Characterization of Mutations in the GTP-binding Domain of IF2 Resulting in Cold-sensitive Growth of Escherichia coli ', Journal of Molecular Biology, vol. 326, no. 2, pp. 543-551 . https://doi.org/10.1016/S0022-2836(02)01367-0
Laursen, B S, Siwanowicz, I, Larigauderie, G, Hedegaard, J, Ito, K, Nakamura, Y, Kenney, J M, Mortensen, K K & Sperling-Petersen, H U 2003, ' Characterization of mutations in the GTP-binding domain of IF2 resulting in cold-sensitive growth of Escherichia coli ', Journal of Molecular Biology, vol. 326 .
Laursen, B S, Siwanowicz, I, Larigauderie, G, Hedegaard, J, Ito, K, Nakamura, Y, Kenney, J M, Mortensen, K K & Sperling-Petersen, H U 2003, ' Characterization of Mutations in the GTP-binding Domain of IF2 Resulting in Cold-sensitive Growth of Escherichia coli ', Journal of Molecular Biology, vol. 326, no. 2, pp. 543-551 . https://doi.org/10.1016/S0022-2836(02)01367-0
Laursen, B S, Siwanowicz, I, Larigauderie, G, Hedegaard, J, Ito, K, Nakamura, Y, Kenney, J M, Mortensen, K K & Sperling-Petersen, H U 2003, ' Characterization of mutations in the GTP-binding domain of IF2 resulting in cold-sensitive growth of Escherichia coli ', Journal of Molecular Biology, vol. 326 .
The infB gene encodes translation initiation factor IF2. We have determined the entire sequence of infB from two cold-sensitive Escherichia coli strains IQ489 and IQ490. These two strains have been isolated as suppressor strains for the temperature-s
Autor:
Brian Søgaard Laursen, Jakob Hedegaard, Juan Manuel Palacios Moreno, Kim Kusk Mortensen, Hans Uffe Sperling-Petersen, S. Steffensen
Publikováno v:
Genes to Cells. 7:901-910
Background: The gene infB encodes the prokaryotic translation initiation factor IF2, a central macromolecular component in the formation of the ribosomal 70S initiation complex. In Escherichia coli, infB encodes three forms of IF2: IF2α, IF2β and I