Fig. 4: Comparison of ex vivo M and recombinant WT AAT.
From: High-resolution ex vivo NMR spectroscopy of human Z α1-antitrypsin
a Comparison of 1H,13C SOFAST-gHMQC spectra (isoleucine regions) of M AAT and U-1H,13C recombinant wild-type AAT (deconvolved using NUWS-NUS44) (298 K, 900 MHz). Resonance assignments are indicated, and green shading highlights the presence of doubled peaks. b Stereo view of combined methyl chemical shift changes, \({\Delta}\delta_{{\mathrm{CH}}} = \sqrt {{\Delta}{\delta}_{\mathrm{H}}^2 + \left( {\Delta}\delta_{\mathrm{C}}/4 \right)^2}\), projected onto the AAT structure72 with the most abundant M6 isoform glycans shown45, modelled using CHARMM-GUI75. Doubled methyl resonances are indicated in green. c Comparison of 1H,13C SOFAST-gHMQC spectra (isoleucine region) of ex vivo M AAT purified from a single donor and from a pool of eight donors.
