Oxidative folding intermediates with nonnative disulfide bridges between adjacent cysteine residues -- Data Supplement - Supporting Figure -- Proceedings of the National Academy of Sciences

Supporting information forČemažar et al. (2003) Proc. Natl. Acad. Sci. USA, 10.1073/pnas.2225470100

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Fig. 5.
Molecular models of three folding intermediates. Superposition of each of the three modeled intermediate species (blue) on the native conformation (red). Dashed lines indicate the disulfide bonds. (A) Stereo view of MFI (1-8, 17-18, 23-31). (B) Stereo-view of I-1 (1-18, 8-17, 23 31) intermediate. (C) Stereo view of I-4 (1-31, 8-18, 17-23) intermediate. The rms deviation values indicated in angstroms were calculated between the cysteine C_α atoms of each intermediate species and the native Amaranthus α-amylase inhibitor after an optimal superposition of the two structures.