Abstract:
The stability of the milk casein is dependent on the presence of Kappa-casein on the surface of the micelle where it serves as an interface between the hydrophobic caseins and the aqueous environment of milk. Crystal structure of Shewanella oneidensis FMN-binding oxidoreductase was chosen as a template for homology modeling of Bovine Kappa-casein (CASK). The N- and C-terminal domains contain mainly α-helices connected by central β-Sheets with three-core α / β/ α Mur CD N-terminal domain. Multiple sequences showed considerable sequence similarity among the mammals family. The highly conserved residues of the template and target were also observed. Ramachandran plot and the energy graph indicated overall good and stable quality of the protein structure. The homology model was well superimposed on the corresponding units of the template. The overall topology and secondary structural elements were quite conserved. The ligands were found to be associated with the segment by hydrophilic, hydrophobic and protein by H2O interactions. The objective was to predict a 3D homology model on the basis of sequence and structural similarity that will fulfill the criteria of a good quality model.
