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. 2008 May 23;283(21):14703–14716. doi: 10.1074/jbc.M800313200

FIGURE 8.

FIGURE 8.

Diagonal plots of inter-residue NOEs in single- and two-chain insulin analogs. A, SCI-57; B, 2CA. More inter-residue NOEs are observed within the insulin moiety of the SCI-57 than in 2CA. Contacts between main chain protons are shown at lower right; side chain-side chain and side chain-main chain contacts are shown at upper left. Red boxes contain contacts from the B3-B5 segment to side chains of A9 and A10 (labeled as a or a′); contacts in blue boxes (b and b′) represent NOEs from the B24-B26 segment to the central B-chain α-helix residue diagnostic of native-like B-chain super-secondary structure. The green box (c in A) contains linker-related NOEs. In SCI, residues 1-57 indicate (i) B1-B30 (residues 1-30), (ii) linker (C1-C6; peptide positions 31-36), and (iii) A1-A21 (residues 37-57). In 2CA, residues 1-51 designate the B-chain (residues 1-30) and A-chain (residues 31-51).