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. Author manuscript; available in PMC: 2018 Mar 26.
Published in final edited form as: J Biomol NMR. 2017 Nov 15;69(3):111–121. doi: 10.1007/s10858-017-0128-3

Fig. 2.

Fig. 2

Plots of experimental data measured on monomeric IL-8(1–66) in solution as a function of residue number. a Chemical Shift Index. b 1H/15N heteronuclear NOE. c Residual Dipolar Couplings used to cross-validate the solution NMR structure of monomeric IL-8 (1–66). The helical region of the protein displays a characteristic Dipolar Wave pattern. d Resonance intensities after incubation of IL-8(1–66) in D2O for 1 h. Peak height was measured for all peaks in a 1H/15N HSQC spectrum and normalized to the peak height of residue Leu49. The locations of proline residues are indicated with a ‘P’