Figure 2.

Molecular simulations of aromatic interactions in the insulin dimer. A, aromatic–aromatic interactions across insulin's dimer interface involve Phe^B24, Tyr^B16, Phe^D24 (sticks) and either Tyr^D26 (left) or Trp^D26 (right). Residues were extracted from T₆ structure 4INS. B, contour maps depicting empirical interaction energies between B26 (Tyr on left and Trp on right) at varying χ₁ and χ₂ angles and the other three residues shown in A. The orientation of Tyr^B26 or Trp^B26 in the WT or variant crystal structure is indicated by a green “x”; orientation of Tyr^B26 or Trp^B26 in the local model is indicated by a green asterisk.