Zobrazeno 1 - 10
of 35
pro vyhledávání: '"Bent W. Sigurskjold"'
Autor:
Lavinia G. Marinescu, Helena Staunstrup Christensen, Christian Pedersen, Tobias Gylling Frihed, Mikael Bols, Bent W. Sigurskjold
Publikováno v:
University of Copenhagen
The efficient synthesis of a new class of cyclodextrin trimers has been carried out by using a click chemistry strategy. The cyclodextrin trimers were subsequently investigated for molecular recognition of peptides with aromatic side chains. Binding
Autor:
Samuel C. Zeeman, Maher Abou Hachem, Martin J. Baumann, Hiroyuki Nakai, Birte Svensson, Bent W. Sigurskjold, Natsuko Nakai, Diana Santelia, Andreas Blennow, Mikkel A. Glaring
Publikováno v:
FEBS Journal. 278:1175-1185
Starch-binding domains are noncatalytic carbohydrate-binding modules that mediate binding to granular starch. The starch-binding domains from the carbohydrate-binding module family 45 (CBM45, http://www.cazy.org) are found as N-terminal tandem repeat
Autor:
Charlotte O'Shea, Johan G. Olsen, Mathilde J. Kaas Hansen, Vincent Goffin, Birthe B. Kragelund, Sophie Bernichtein, Bent W. Sigurskjold
Publikováno v:
Journal of Molecular Recognition. 24:533-547
The cytokine hormone prolactin has a vast number of diverse functions. Unfortunately, it also exhibits tumor growth promoting properties, which makes the development of prolactin receptor antagonists a priority. Prolactin binds to its cognate recepto
Autor:
Marco van de Weert, Svend Havelund, Kasper Huus, Sven Frokjaer, Helle Birk Olsen, Bent W. Sigurskjold
Publikováno v:
Biochemistry. 45:4014-4024
The influence of ligand binding and conformation state on the thermostability of hexameric zinc-insulin was studied by differential scanning calorimetry (DSC). The insulin hexamer exists in equilibrium between the forms T6, T3R3, and R6. Phenolic lig
Autor:
Bent W. Sigurskjold, Eva Johansson, Mathias Fanø, Sine Larsen, Ulla Christensen, Jan Neuhard, Julie H. Bynck, Martin Willemoës
Publikováno v:
Journal of Biological Chemistry. 280:3051-3059
dCTP deaminase (EC 3.5.4.13) catalyzes the deamination of dCTP forming dUTP that via dUTPase is the main pathway providing substrate for thymidylate synthase in Escherichia coli and Salmonella typhimurium. dCTP deaminase is unique among nucleoside an
Autor:
Birte Svensson, Birgit C. Bønsager, Bent W. Sigurskjold, Peter Kresten Nielsen, Carolyn R. Berland
Publikováno v:
Biochemistry. 42:1478-1487
The kinetics and energetics of the binding between barley alpha-amylase/subtilisin inhibitor (BASI) or BASI mutants and barley alpha-amylase 2 (AMY2) were determined using surface plasmon resonance and isothermal titration calorimetry (ITC). Binding
Autor:
Jonas Heilskov Graversen, Søren K. Moestrup, Bent W. Sigurskjold, Rikke Høegh Lorentsen, Hans Christian Thøgersen, Christian Bøtcher Jacobsen, Michael Etzerodt
Publikováno v:
Journal of Biological Chemistry. 275:37390-37396
C-type lectin-like domains are found in many proteins, where they mediate binding to a wide diversity of compounds, including carbohydrates, lipids, and proteins. The binding of a C-type lectin-like domain to a ligand is often influenced by calcium.
Publikováno v:
Biochemistry. 38:6300-6310
The stability of three forms of glucoamylase from Aspergillus niger has been investigated by differential scanning and isothermal titration calorimetry: Glucoamylase 1 (GA1), which consists of a catalytic domain and a starch-binding domain (SBD) conn
Autor:
Søren K. Moestrup, Michael Etzerodt, Jonas Heilskov Graversen, Christian Jacobsen, Hans Christian Thøgersen, Bent W. Sigurskjold, Rikke Høegh Lorentsen
Publikováno v:
Journal of Biological Chemistry. 273:29241-29246
Tetranectin, a homotrimeric protein belonging to the family of C-type lectins and structurally highly related to corresponding regions of the mannose-binding proteins, is known specifically to bind the plasminogen kringle 4 protein domain, an interac
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