After 14 ns WT structure exhibited minimum deviation till the end of simulation that is 40 ns with its backbone RMSD ranging from ∼0.14 to ∼0.22 nm, where as mutant structure showed maximum deviation till the end of simulation resulting backbone RMSD of ∼0.13 to ∼0.47 nm respectively.
The E178Q +Put) mutant structure shows some interesting differences.
The modelled native RpoS and mutant RpoS structures showed good stereochemical properties, with 92.0% and 85.4% of the residues being within the most favourable region of the Ramachandran plot, respectively, whereas the native and mutant TviE showed 86.5% and 80.0% of the residues in most favourable region of the plot, respectively.
Native and mutant (R326H and R356Q) Tyrp1 structures showed the g-factor in the ranges of 0.40, 0.45, and 0.46, respectively.
Moreover the native structure shows highest atomic density distribution of 41.9 nm−3 but mutant (R326H and R356Q) structures showed 52.2 and 52.3 nm−3, respectively, (Table 4).
In Figure 4, both mutant (R326H and R356Q) structures showed an increase in helical content which leads to became more rigid on conformation.
Native and mutant (R326H and R356Q) structures showed similar fashion of deviation till 12000 ps from the initial structure, but after this native structure showed greater value of SASA than mutant (R326H and R356Q) structures.
In Figure 2(a), native and both mutant (R326H and R356Q) structures showed similar way of deviation till 3050 ps from their starting structure, resulting in a backbone RMSD of ~0.14 to 0.52 nm during the simulations.
The average Rg value was 1.84 nm in native, whereas the mutant R326H and R356Q structures showed average Rg value of 1.81 and 1.79 nm, respectively, signified in Table 4.
It indicates that both mutant (R326H and R356Q) structures showed an increase in helical content and total absence in β-sheet in the amino acid residual position from 150 to 170 and 5 to 20, respectively.
