RESUMO
In the title compound, [Cu(C(15)H(11)N(3)O(3))(C(10)H(8)N(2))], the Cu(II) atom is five-coordinated in a distorted square-pyramidal CuN(3)O(2) geometry. The basal positions are occupied by three donor atoms from the tridentate Schiff base ligand and by one N atom from the 2,2'-bipyridine ligand. The axial position is occupied by the other N atom of the 2,2'-bipyridine ligand. The crystal structure is consolidated by weak C-Hâ¯O hydrogen bonds. In addition, π-π inter-actions between adjacent pyridine rings (centroid-centroid distances = 3.238 and 3.313â Å) may also stabilize the crystal packing.
RESUMO
The recombinant allergen, Bla g 2, was expressed by prokaryotic vector E. coli and eukaryotic vector P. Pastoris. The different structures and configurations of the Bla g 2 from E. coli and P. Pastoris were studied by fluorescence and circular dichroism. The secondary structures of Bla g 2 in solution, and the composition besides the type of its tertiary structure were proposed. These studies help understand the differences between prokaryotic and eukaryotic expression systems, reveal the relationship between the structure and the function of Bla g 2, and improve the production of this significant allergen.
Assuntos
Alérgenos/química , Ácido Aspártico Endopeptidases/química , Dicroísmo Circular/métodos , Baratas/química , Expressão Gênica , Alérgenos/genética , Alérgenos/imunologia , Animais , Ácido Aspártico Endopeptidases/genética , Ácido Aspártico Endopeptidases/imunologia , Baratas/genética , Baratas/imunologia , Escherichia coli/genética , Escherichia coli/metabolismo , Proteínas de Insetos/química , Proteínas de Insetos/genética , Proteínas de Insetos/imunologia , Pichia/genética , Pichia/metabolismo , Estrutura Secundária de ProteínaRESUMO
Recombinant proteins extracted from inclusion body remain in denaturation status. Renaturation in vitro after initial purification is a key step of downstream processing. A common method of renaturation of recombinant proteins is the dilution method. With Bla g 2 as a model protein, the conformational changes of denatured and renatured Bla g 2 were investigated by applying fluorescence spectra. The effects of different urea concentrations, different SDS concentrations and different pH on the fluorescence intensity of renatured protein were also investigated. The reasons for these were studied with the knowledge of molecular structure.
