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. Author manuscript; available in PMC: 2011 Jan 14.
Published in final edited form as: J Phys Chem B. 2010 Jan 14;114(1):531. doi: 10.1021/jp9083635

Figure 1.

Figure 1

Cartoon representation of the organophosphorous hydrolase structure adsorbed onto the functionalized mesoporous silica surface. (A) Top view of the OPH dimer. Regions of large atomic fluctuations in the MD simulations are indicated in violet (L1, residues 155-165), blue (L2, residues 172-182), yellow (L3, residues 201-215), orange (L4, residues 230-240), purple (L5, residues 255-275) and green (L6, residues 306-325) for only one monomer. (B) Close-up view of the active site pocket with residues represented in licorice and Zn2+ cations in the Corey–Pauling–Koltun (CPK) model (yellow). The residue Y309 in the gateway to the active site pocket is highlighted. (C) Side view of the OPH dimer. Positively charged residues in the protein that interact with the functionalized mesoporous silica are represented in licorice. The functionalized mesoporous silica is represented in CPK (red). The explicit model water molecules are omitted for clarity of visualization.