FIGURE 9.

MD-based model of μIR/3-[iodo-Tyr^B26]insulin interface assuming neutral iodine. A, time evolution of the I···R distance (distance of Tyr^B26-I to the interacting insulin/μIR residues). The upper and lower panels show the increase of the I···O=C(Val-365), I···H-N(Arg-61), and I···H-N(Gln-81) bond lengths, respectively, and the decrease of the I···C_γ(Lys^B29), I···H-NE(His-79), I···C_α(Pro^B28), and I···O=C(Thr^B27) bond lengths in the course of the MD simulation. The black dashed line at 150 ps represents the point when the electrostatically driven interactions dissociate and the van der Waal-driven interactions form. B, snapshot structure of 3-[iodo-Tyr^B26]insulin bound to the μIR. Only the residues interacting with 3-I-Tyr^B26 are illustrated. Bond formation/dissociation with the iodine atom are shown as full and dashed line arrows, respectively.