Browsing by Subject "Bioinformatic Methods"

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  • Jasim, Muhammad (Helsingin yliopisto, 2020)
    Tiivistelmä – Referat – Abstract Proteins differ from one another on the basis of their amino acid sequences, display a different spatial shape and structure, and have different functions. The linear order of amino acid residues are chained to one another by peptide bond. The ß-strands and α-helices can be considered as the key components present in the three-dimensional structure of a protein. There are several bioinformatic methods involved to predict structure and function of protein such as searching sequencing similarities, multiple sequence alignment, characterisation of domains, solvent accessibility, and modelling three-dimensional structures at atomic level. The main focus of this study was to build the three-dimensional structure models and then compare the homologues regions in different models. 36 reviewed capsid L1 and L2 protein sequences of human papilloma virus subtypes were selected based on 65% sequences similarity from Universal Protein database. We utilised several computational algorithms in this study for the analysis of protein sequences for the evolutionary relationship and modelled the three-dimensional structures of capsid L1 and L2 proteins of oncogenic human papilloma virus subtypes. For domains analysis in the protein sequences, we used Simple Modular Architecture Research Tool algorithms and predicted secondary structure of protein using Protein Prediction Protein 4.0 tool. I-TASSER Iterative threading assembly refinement algorithms were utilised for three-dimensional structure modelling of capsid L1 and L2 proteins. We found out a different evolutionary relationship and conserved residues in capsid L1 protein of human papilloma virus and L2 protein of human papilloma virus, and their different level of effect on the protein structure. We also predicted three-dimensional structure models for capsid L2 protein of human papilloma virus subtypes 41 and 13 which are folded completely differently from the rest L2 proteins. X-ray crystallography study is suggested for the determination of three-dimensional structure of L2 protein for understanding their contribution in viral assembly process.