Figure 5: Flexibility of wild-type and mutant TKs.
From: Two strategies to engineer flexible loops for improved enzyme thermostability
(A) Comparison of wild-type and mutant TKs structures coloured by normalized RMSF at 300 K and 370 K. Each structure was achieved from the average of the last 10-ns trajectory of one simulation. The surfaces of loops8, 13, 15, 21 are displayed and only those of WT at 300 K are labelled. (B) The RMSD of loops8, 13, 15 of wild-type and mutant TKs with the average conformations of last 10 ns as reference. For H192P/A282P, RMSD of loops8 and 15 were combined. Only the RMSD values of frames at 10-ps intervals were displayed for clarity and each value was the average of RMSD from triplicate simulations.
