Analyses on the side-chains of the hydrophobic core residues in the wt-hPAH and in the mutants.

<p>A) Distances between pairs of selected hydrophobic core residues (Leu37, Phe39, Leu41, Val51, Phe55, Ile65, Phe79, Leu91, Ile94, Leu98) were calculated as the minimum over all possible pairs of non-hydrogen atoms of the side chain. Average values calculated over the 50-ns simulation are reported. B) Time evolution of the solvent accessible surface area (SASA) of Phe55 (black) and Val60 (green) in the F39C mutant (left, top). Time evolution of the SASA of the residue in position 65 in the I65S (yellow), I65T (violet) and I65V (cyan) mutants (left, bottom).