Improving macromolecular electrostatics calculations

Autor: Jens Erik Nielsen, Kim Vilbour Andersen, Gerrit Vriend, Rebecca C. Wade, Barry Honig, Gerhard Klebe, Rob Hooft

Publikováno v: Protein Engineering, Design and Selection. 12:657-662

Electrostatic interactions play a key role in many aspects of protein engineering. Consequently, much effort has been put into the design of software for calculating electrostatic fields around macromolecules. We show that optimization of hydrogen bo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::6a83356a4fbc187c3780b56826b0cde6
https://doi.org/10.1093/protein/12.8.657

Conserved Residues and Their Role in the Structure, Function, and Stability of Acyl-Coenzyme A Binding Protein

Autor: Karsten Kristiansen, Thomas B. Neergård, Trausti Baldursson, Jens Knudsen, Jan Jepsen, Birthe B. Kragelund, Jenny B. Krøll, Flemming M. Poulsen, Kim Vilbour Andersen, Keld Poulsen, Peter Roepstorff

Publikováno v: Kragelund, B B, Poulsen, K, Andersen, K V, Baldursson, T, Krøll, J B, Nergaard, T B, Jepsen, J, Roepstorff, P, Kristiansen, K, Poulsen, F M & Knudsen, J 1999, ' Conserved residues and their role in the structure, function and stability of acyl-Coenzyme A binding protein ', Biochemistry, vol. 38, pp. 2386-2394 . https://doi.org/10.1021/bi982427c

In the family of acyl-coenzyme A binding proteins, a subset of 26 sequence sites are identical in all eukaryotes and conserved throughout evolution of the eukaryotic kingdoms. In the context of the bovine protein, the importance of these 26 sequence

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a7d90b8aebbdddcb91d5cca17e05a941
https://doi.org/10.1021/bi982427c

Structure of the Bacillus agaradherans Family 5 Endoglucanase at 1.6 Å and Its Cellobiose Complex at 2.0 Å Resolution

Autor: Martin Schülein, M.E Bjornvad, M. Dauter, Gideon J. Davies, Andrzej M. Brzozowski, Kim Vilbour Andersen

Publikováno v: Biochemistry. 37:1926-1932

The enzymatic degradation of cellulose, by cellulases, is not only industrially important in the food, paper, and textile industries but also a potentially useful method for the environmentally friendly recycling of municipal waste. An understanding

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc80a4f0734b17c80bb22d360391e201
https://doi.org/10.1021/bi972162m

Thermodynamics of Ligand Binding to Acyl-Coenzyme A Binding Protein Studied by Titration Calorimetry

Autor: Jens Bjerre Knudsen, Kim Vilbour Andersen, Nils J. Færgeman, Birthe B. Kragelund, Bent W. Sigurskjold

Publikováno v: Færgeman, N J, Sigurskjold, B W, Kragelund, B B, Andersen, K V & Knudsen, J 1996, ' Thermodynamics of Ligand Binding to Acyl-Coenzyme A Binding Protein Studied by Titration Calorimetry ', Biochemistry, vol. 35, no. 45, pp. 14118-14126 . https://doi.org/10.1021/bi960545z

Ligand binding to recombinant bovine acyl-CoA binding protein (ACBP) was examined using isothermal microcalorimetry. Microcalorimetric measurements confirm that the binding affinity of acyl-CoA esters for ACBP is strongly dependent on the length of t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b46f0124a54f22ca792d171d3bfcafa0
https://doi.org/10.1021/bi960545z

Three-dimensional Structure of the Complex between Acyl-Coenzyme A Binding Protein and Palmitoyl-Coenzyme A

Autor: F.M. Poulsen, Jens Knudsen, Birthe B. Kragelund, Jens Chr. Madsen, Kim Vilbour Andersen

Publikováno v: Journal of Molecular Biology. 230:1260-1277

Multidimensional 1H, 13C and 15N nuclear magnetic resonance spectroscopy has been used to study the complex between palmitoyl-coenzyme A and acyl-coenzyme A binding protein. The 1H and the 15N spectra of the holo-protein have been almost completely a

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7451aaa13033e5107dd1801b66dbc44d
https://doi.org/10.1006/jmbi.1993.1240