Fig. 5: Comparison of wild-type (M), Z and S AAT variants.
From: High-resolution ex vivo NMR spectroscopy of human Z α1-antitrypsin
a–c Comparisons of ex vivo NMR observations of M AAT with those of the Z variant, and d–f with the S variant. a, d Overlays of 1H,13C SOFAST-gHMQC spectra (isoleucine region) for M, Z and S AAT, with resonance attributions indicated. Contour levels are normalised for concentration and acquisition time. b, e Combined methyl chemical shift changes between wild-type and variant AAT, \({\Delta}\delta_{{\mathrm{CH}}} = \sqrt {{\Delta}{\delta}_{\mathrm{H}}^2 + \left( {\Delta}\delta_{\mathrm{C}}/4 \right)^2}\), projected onto the wild-type structure72. Resonances whose attribution could not be traced are indicated in dark grey, and mutations in the Z and S variants are indicated with magenta and green spheres, respectively. Colouring of secondary structure elements is consistent with Fig. 1b. c, f Intensity changes between M and Z/S variants of AAT, projected onto the wild-type recombinant AAT structure72.
