Figure 1

Molecular graphics view of explicit membrane systems at $\tau =12°$ (left) and 40° (right). WALP19 is shown in yellow with $N$ terminus in blue and $C$ terminus in red, lipid chains in white, and water in light blue.Reuse & Permissions

Figure 2

(a) (solid) Total PMF after correction of limited sampling of helix precession and (thick dot line) uncorrected PMF. The accessible tilt angles at 303.15 K are below the dashed line. (b) Decomposition of the total PMF into two contributions from the direct helix-environment interaction (${\mathcal{W}}_{\mathrm{env}}$) and the helix conformation itself (${\mathcal{W}}_{\mathrm{conf}}$). The helix precession entropy contribution (${\mathcal{W}}_{\mathrm{pre}}$) is shown for comparison with ${\mathcal{W}}_{\mathrm{conf}}$. (c) Individual residue contributions to ${\mathcal{W}}_{\mathrm{conf}}$ (excluding ${\mathcal{W}}_{\mathrm{pre}}$). The numbers in lines represent the residue numbers (2 to 18), and $T$ symbol (thick solid line) for the total contribution from two terminal groups (Gly1 and Ala19). The contributions from the four interfacial Trp residues are shown by thick dashed lines (2, 3, 17, and 18).Reuse & Permissions

Figure 3

Average locations of sidechains of Trp2 (solid), Trp3 (dashed), Trp17 (short dashed), and Trp18 (dot line) as a function of $\tau$. Thin lines represent corresponding profiles by tilting an ideal $\alpha$-helical WALP19.Reuse & Permissions

Figure 4

Average density profiles calculated over all the tilt angles: methylene ${\mathrm{CH}}_2$ (solid), glycerol (dashed), ${\mathrm{PO}}_4$ (dashed dot), ${\mathrm{H}}_2\mathrm{O}$ (double dashed), and Trp (thick solid line). Two vertical lines approximately represent the membrane hydrophobic-hydrophilic interface.Reuse & Permissions