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