Molecular Dynamics Simulation Comparison of BRAF Kinase protein mutants

Among all of the deadly diseases, Glioma Blastoma is one of the most harmful diseases and the prevalence rate of its frequency is increasing day by day. This research addrsses the structural study of the BRAF kinase protein.  From previous research, it is seen that there is a mutation in the position 600 in the BRAF kinase protein in which Valine(V) should be present; when the mutation occurs in this position to other amino acid specifically Glutamic acid ( E ), this leads to this harmful disease Glioma Blastoma. This study consists of a molecular dynamics simulation comparison of BRAF kinase protein mutants. There are two more mutations which occur very frequently in this position: Aspartic Acid (V600D) and Glycine (V600G). Molecular docking is also done with the ligand diarylthiazole of pdb_id 4CQE and several hydrogen bonding and Vanderwaal  interactions are found amongst which interaction of Wild type BRAF protein with diarylthiazole is seen with strongest value -7.2kj/mol. The data generated from this research can be used for further research on molecular simulation studies of BRAF protein mutants