Figure 6.

Energetics of adsorption of Rsn-2 to an ideal interface. (A) Schematics of the coarse-graining (CG) from the all-atom NMR structure (AA), and typical Rsn-2 configuration at different adsorption stages: in bulk (state 0, corresponding to the native structure); with the flexible N-terminal region adsorbed at the interface (state 1); and fully adsorbed and partially unfolded in side-view (top) and top-view (bottom) (state 2). The N-terminal tail (residue IDs 1–15) is shown in blue, the α-helix (16–38) in purple, the β-sheet (45–88) in yellow, and the loop (39–44) and the C-terminal tail (89–96) are in gray. The interface is represented by the black wavy line. For the coarse-grained structures we only show the C_α beads and not the side chains. (B) Energy of interaction with the interface for a typical adsorption event, showing the energetic contributions from the N-terminus (residues 1–15; dashed cyan line) and the globular region of the protein (residues 16–96; dashed blue line) to Rsn-2 adsorption (purple line). (C) Fraction of native contacts corresponding to the α-helix and the β-sheet (green line) and those involved in the formation of the hydrophobic core (dashed pink line). The first adsorption step involves no loss of native contacts, whereas the second step involves the disruption of the hydrophobic core while the secondary structure elements are conserved. To see this figure in color, go online.