Figure 5.

NMR solution structure of peptide R2.0.NMR spectra of R2.0 and the most relevant NMR data used for secondary structure determination. A) ¹H NMR spectrum of R2.0 in H₂O/CD₃CN 80:20 (v/v). Inset: amide proton region of the spectrum. B) NOESY contour plot of the amide-aliphatic proton region. C) NOESY contour plot of the amide proton region. D) Summary of sequential, short- and medium-range connectivities for R1.5G3. Thickness of solid bars indicates relative intensity of the NOEs, i.e., weak, medium and strong. Shaded bars indicate connectivity observed to the CδH of a proline residue in place of the NH. X at positions 28 and 30 corresponds to 1Nal and ornithine, respectively. E) Ensemble of 15 NMR solution structures of R2.0 with the lowest DYANA target functions after energy minimization. Backbone atom superposition of the Phe12-Ile15 segment over the corresponding residues of full-length RANTES; the backbone of the N-terminal hydrophobic patch is shown as a blue tube; side chains are shown as sticks. F) Backbone atom superposition of the Tyr27-Tyr29 segment over the corresponding residues of full-length RANTES; the backbone of the C-terminal hydrophobic patch is shown as a red tube; side chains are shown as sticks. G) Simultaneous Phe12-Ile15 (blue tube) and Tyr27-Tyr29 (red tube) Cα atom superposition of the 15 NMR solution structures onto the Phe12-Ile15 and Tyr27-Tyr29 of full length RANTES (11–29 aa stretch of RANTES is shown as a green tube). Figure was generated using VMD.