In Y493H, we have observed quite a rich feature in the RMSD plot due to conformation change in the protein. The average RMSD value of 1.45Å is observed in the corresponding trajectory up to 85ns, and then the switching of the confirmation occurs. Subsequently, other conformational changes are observed at 155ns (Fig. ). The primary reason behind these confirmation switches is the change in the protein's secondary structure, which has been described in section 3.3. The RMSD value increases when going from the turns to coils. The signature of the conformation change is captured in the probability distribution plot as well.