Fig. 4: Structural analysis of CALB in different IL microenvironments.

a Superimposed cartoon representation of the overall structures of CALB from the cluster analysis based on equilibrium trajectories drived from three independence MD simulations in each system. b RMSD of the enzyme backbone with respect to the initial structure as a function of time, the statistical numbers came from three independence simulations. c Averaged RMSD of individual residues determined from three independence simulations with the last equilibrium 100 ns trajectory for each simulation. d Fluorescence spectra. e Far-UV CD spectra. f Calculated width of catalytic cavity entrance between two gating residues (error bars represent standard deviation, n = three independence simulations), ILE189 and ILE285. g Snapshots of the active site cavity structure (derived from cluster analysis) of CALB binding with different PEG backbones. The enzyme surface is shown in gray, CALB pocket in violet, ILE189 and ILE285 in orange, and PEG backbones in green, purple or yellow. h Spatial distribution of substrate molecules (1-phenylethyl alcohol) occupancy at the surface of CALB from the equilibrium 100 ns in three independence simulations for each system.