Fig. 7From: Identification and structural analysis of a thermophilic β-1,3-glucanase from compostMolecular dynamics simulations reveal the dynamic differences among WT and its mutants. A After 300 ns, all the proteins are in equilibrium with similar RMSD. B RMSF comparison shows that the loop region (residues 156–174) in C160G is most dynamics, and the region in WT is most rigidBack to article page