Figure 4

Colour-coded sequences of the ratio of folded and unfolded SASA for [PDB:5cro] and [PDB:1ucj]. Upon folding, most residues tend to be less exposed to solvent than in the unfolded state, as shown by the majority of reddish residues in the figure. However, some residues may be more exposed in the folded state (bluish residues). a) Tyr 26 (labelled) of [PDB:5cro] has a ratio of folded SASA over unfolded SASA in the range 0.9–1.1, suggesting that no reverse hydrophobic effect is taking place (see text). b) Thr 36 (labelled) of [PDB:1ucj], as most residues, is also in a reddish shade. Since this residue bears a polar side chain, its burial is suggestive of a destabilizing contribution to the native conformation. The data shown in both cases is for 1.4 Å of solvent radius and 2000 conformations.