| In the present work, we used homology-modeling techniques to investigate the structural/functional relationships of three proteins: apolipoprotein B-100, haptoglobin, and haptoglobin-related protein and a group of mitoriboprotein. At times detailed, structures can be resolved using experimental techniques, but these methods can be difficult and time consuming. It is therefore beneficial to predict a structural model of a protein in order to better understand its structure/function relationships and help guide experimental research. Homology modeling is a quick and accurate method for generating structural models. This method uses comparative analysis and known protein structures to generate models of homologous proteins.; In apolipoprotein B-100, the model was able to help explain how the molecule was able to fold and to start building a lipid particle. The model also provided insight into how that protein changed conformation as the lipid particle grew. Circular dichroism and Fourier transform infrared spectroscopy confirmed the secondary structure of the haptoglobin model, whereas mass spectroscopy confirmed the model's placement of disulfide bonds in the haptoglobin tetramer. The model also offered insight into the potential hemoglobin-binding domain. The haptoglobin-related protein model indicated potential regions that might be responsible for its lytic activity against trypanosomes. Finally, homology modeling was used to create models of 16 mitoriboprotein to be fitted in the electron density map of the large subunit of bovine mitochondria ribosome. It is hoped that this model will provide insights into the function of the mitoriboproteins and the evolution of the mitoribosome. |
