Figure 4: MD simulation of TXAS protein and expression of TXAS mutants.
From: Probing water micro-solvation in proteins by water catalysed proton-transfer tautomerism
(a) TXAS homology structure shows the characteristic P450 fold, illustrating the phenylalanine residues (yellow), five tryptophan positions (green) and haem (stick figures in violet). (b) The solvent-accessible surfaces of the active site cavities calculated using an H probe under an electrostatic potential (ESP) surface with electrophile/nucleophile (blue/red). Proposed gating channels are indicated. (c) The local environment of tryptophan (W) in hydrated TXAS (or water), in which W is shown in green, water is blue, acidic residues are red, hydrophobic residues are yellow and other residues are white. (d,e) Emission spectra of various TXAS mutants excited at 310 nm. The use of two separated figures is to avoid spectral congestion. (f) Emission spectra of denatured (2,7-aza)Trp31,65,133,203,446-TXAS and the decomposed PL spectra.
