Figure 3
From: Folding and Stabilization of Native-Sequence-Reversed Proteins
(a) Structure of native α3D; hydrophobic residues are shown as vdW spheres. (b) Structure of sequence-reversed α3D. (c) Solvent accessible surface areas (SASAs) of sequence-reversed and native α3D structures and their component hydrophobic residues. Hydrophobic residues within the reverse sequence stay buried throughout the simulation, featuring a SASA comparable to that associated with native α3D (particularly with respect to the crystal structure).
