List of figures
  1. Figure 1: Protein expression analysis using PaxDB database.
  2. Figure 2: Sequence alignment of full-length IRX proteins using Clustal omega
  3. Figure 3: IRX protein sequences and their conservation.
  4. Figure 4: Secondary structure prediction and homology model of IRX4 homeodomain
  5. Figure 5: Representation of the energy minimized models of IRX4 homeodomain bound to DNA generated using UCSF Chimera.
  6. Figure 6: The interaction profile of WT IRX4 homeodomain and its interaction with DNA before and after MD simulations.
  7. Figure 7: A statistical representation of the distribution of somatic mutations in the IRX4 full-length protein and the homeobox region .
  8. Figure 8: The representative RMSF values of native IRX4 homeodomain protein structure and the mutants.
  9. Figure 9: DSSP plots for secondary structure transitions in IRX4 WT and variants in the N-terminal region during MD simulations.
  10. Figure 10: DSSP plots for secondary structure transitions C-terminal variants during MD simulations.
  11. Figure 11: Average free energy of binding per nucleotide in the DNA for all variants.List of tables
  1. Table 1: Physicochemical parameters computed using ProtParam tool
  2. Table 2: Predicting the stability of mutant proteins by I-Mutant Server
  3. Table 3: Decomposition of calculated binding energies using MM/GBSA
  4. Table 4: The hydrogen bonds between WT IRX4 homeodomain and DNA
  5. Table 5: Hydrogen bonds in the homeodomain mutants
  6. Table 6: Prediction of the cell-penetrating ability of homeodomain sequence
  7. Table 7: Prediction of cell-penetrating ability of mutant homeodomain