Fig. 4.

Secondary chemical shifts of backbone resonances versus residue number of β2-m in the native state at pH 6.5. (A) ΔCα, (B) ΔCβ, and (C) ΔHα. The locations of secondary structures obtained from the X-ray structure and Cys residues are indicated. The locations of highly (more than 24 h) and moderately (at least 10 min) protected amide protons are indicated by closed and open bars, respectively, under the locations of secondary structures. The chemical shift of the random coil was calculated on the basis of the previous report by Wishart et al. (1995).