Figure 7.

Exposure of W107. Final structures (20 ns) are shown from the MD simulations at 300 K (left), 400 K (middle), and 500 K (right). W107 is shown in VDW and the SASA of the region formed by residues L148-F165 in transparent gray. The color code for the helices is the same as in Figure 1. At 300 K, W107 remains buried and its aromatic rings are perpendicular to Lp7-8. At 400 K, W107 is more exposed, and its aromatic rings are almost parallel to Lp7-8. At 500 K, W107 is mostly exposed. The hydrophobic and aromatic residues in BH2 (W151, I152, W158, L161, L161, Y164, and F165) are shown in Licorice. [Color figure can be viewed in the online issue, which is available at wileyonlinelibrary.com.]