Fig. 4: NMR binding studies. | Nature Communications

Fig. 4: NMR binding studies.

From: Probing altered receptor specificities of antigenically drifting human H3N2 viruses by chemoenzymatic synthesis, NMR, and modeling

Fig. 4

a 1D 1H-STD NMR. Spectra obtained for the complexes of HK68, NL91, and NL03 HAs with the glycan 2, and inset of the acetyl region. b 19F-R2 NMR. Comparison of transverse 19F relaxation rate, R2(19F), for the fluorinated probe (6) in the absence or presence of the different HA proteins. Addition of competitor molecules 7 and 2 causes a decrease in R2(19F) proportional to their affinities relative to the probe compound 6. The bars represent the average of three replicates ± SD.

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