Solution structure of deglycosylated human IgG1 shows the role of CH2 glycans in its conformation

Spiteri V Doutch J, Rambo R, Gor J, Dalby P, Perkins S, Biophysical Journal (2021) DOI

SASDKC8 – Immunoglobulin G1 (IgG1) Deglycosylated

Immunoglobulin G subclass 1
MWexperimental 144 kDa
MWexpected 148 kDa
VPorod 271 nm3
log I(s) 9.98×10-1 9.98×10-2 9.98×10-3 9.98×10-4
Immunoglobulin G subclass 1 small angle scattering data  s, nm-1
ln I(s)
Immunoglobulin G subclass 1 Guinier plot ln 9.99×10-1 Rg: 5.2 nm 0 (5.2 nm)-2 s2
(sRg)2I(s)/I(0)
Immunoglobulin G subclass 1 Kratky plot 1.104 0 √3 sRg
p(r)
Immunoglobulin G subclass 1 pair distance distribution function Rg: 5.3 nm 0 Dmax: 18.4 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Immunoglobulin G subclass 1 CUSTOM IN-HOUSE model
Synchrotron SAXS data from solutions of Immunoglobulin G1 (IgG1) Deglycosylated in 20 mM L-histidine, 138 mM NaCl, and 2.6 mM KCl buffer, pH 6 were collected on the B21 beam line at the Diamond Light Source storage ring (Didcot, UK) using a Pilatus 2M detector at a sample-detector distance of 4 m and at a wavelength of λ = 0.12 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 4.29 mg/ml was measured at 20°C. 30 successive 30 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Immunoglobulin G subclass 1 (IgG1)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Unknown
Mon. MW   148.4 kDa
Sequence   FASTA