| Comments |
Supporting online material page 6:"[Investigators] analyzed the amount of residual secondary structure in the unfolded state by determining the percentage of residues that are found in either helical or sheet structure in the unfolded state. Table S2 below shows these percentages for the 12 proteins. There is very little formation of sheet structure in the unfolded state apart from in NuG2, where the designed and very stable hairpin 1 is highly formed even in the unfolded state. In most of the proteins that have native state helices, ≈10–25% of residues form helices in the unfolded state. The major outlier appears to be the λ-repressor, for which there is a very large amount of residual helix in the unfolded state." See note beneath table |