Figure 6.

Structure of YscU_CN in complex with SDS micelles computed from NMR restraints. (A) Occupation of different secondary-structure conformations by each residue, averaged over the structure ensemble. Red, α-helix; dashed yellow, 3₁₀ helix; dashed green, turn; dash-dotted black, bend or coil. (B) Backbone alignments for helices 1–3, showing an ensemble of 20 low-energy conformers. Backbones are rendered as golden coils. Positions of C^α atoms at the edges of the aligned segments corresponding to the helix boundaries are marked with green dots and labeled with arrows. (C) View along the long axis (from C to N terminus) of the first three helices of YscU_CN, emphasizing amphipathic helical residue distributions. Backbone atoms are rendered as orange coils and side chains in ball-and-stick format colored according to residue polarity and charge: blue, basic (H, K, and R); red, acidic (D and E); green, polar (S and Q); black, = nonpolar (I, F, M, and Y). Molecular structures were aligned and rendered with the VMD program (51).