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

SASDKB8 – Immunoglobulin G1 (IgG1) Glycosylated

Immunoglobulin G subclass 1
MWexperimental 148 kDa
MWexpected 148 kDa
VPorod 269 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 9.98×10-1 Rg: 5.1 nm 0 (5.1 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: 5.2 nm 0 Dmax: 17.5 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) Glycosylated 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 3.60 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