Fig. 6From: Improving the thermostability of Pseudoalteromonas Porphyrae κ-carrageenase by rational design and MD simulationMolecular dynamics and conformational stability analysis of κ-carrageenase. (a–c) RMSD (a), Rg (b), and RMSF (c) of S190R and WT at 323 K. (d and e) The flexibility changes of S190R relative to WT at 323 K (the changes exceeded 0.05 nm). Red was the area where flexibility increases, and blue was the area where flexibility decreases. The catalytic triad was represented by yellow sticks, while the residues with flexibility increased (Q170, K171 and N173) were represented by blue sticks in Fig. 6eBack to article page