Akademik Veri Yönetim Sistemi
14th National Biomedical Engineering Meeting, İzmir, Türkiye, 20 - 22 Mayıs 2009, ss.498-501
Estimation of disordered regions in proteins as a measurement of flexibility is important in terms of playing key roles in regulation of transcription and translation, protein-protein, protein-DNA interactions and also in determining the tertiary structure of the proteins. It has been determined that proteins that include intensive amounts of aminoacids such as alanine, glycine and proline have propensity of disorder on account of changing Phi and Psi bond angles. In this study, two proteins, one with high propensity of disorder and the other with low propensity of disorder, have been chosen to emphasize the differences between them. The disordered regions in two important enzymes (DNA-topoisomerase I and glutathione peroxidase 5) chosen from the protein bank of ExPasy (Expert Protein Analysis System) have been estimated by using 5 newly developed bioinformatics tools (RONN, FoldIndex, VSL2 DisProt, GlobPlot, DisEMBL). Some proteins that include disordered regions have been related to some metabolic diseases such as diabetes, cancer, Alzheimer. The main aim of this study is to introduce the developed bioinformatics tools related to disordered regions in two selected proteins.