Figure 7 | Scientific Reports

Figure 7

From: Thermostabilization of VPR, a kinetically stable cold adapted subtilase, via multiple proline substitutions into surface loops

Figure 7

(A) Superimposed closeup of the N-terminals of VPR (light blue) (PDB ID: 1SH7) and AQUI (orange) (PDB ID: 4DZT) comparing the H-bond potential of both enzymes (red lines H-bonds in AQUI and blue lines H-bonds in VPR). (B) Closeup of the part of the protein in the closest vicinity of the N238P and T265P mutations in the structure of VPR. (C) Closeup highlighting the residues making up a part of the hydrophobic core and N-terminal interface to the main part of the protein in the structure of VPR. Calcium ions are shown as green spheres for VPR and golden spheres for AQUI. Atomic specifiers for side chains are as follows: carbon atoms are coloured same as the secondary structure; nitrogen atoms are coloured blue; oxygen atoms are coloured red and sulphur atoms coloured yellow.

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