Using atomistic solution scattering modelling to elucidate the role of the Fc glycans in human IgG4.

Spiteri VA, Doutch J, Rambo RP, Bhatt JS, Gor J, Dalby PA, Perkins SJ, PLoS One 19(4):e0300964 (2024) Europe PMC

SASDLY2 – Immunoglobulin G4 (IgG4) Glycosylated

Immunoglobulin G subclass 4
MWexperimental 147 kDa
MWexpected 145 kDa
VPorod 256 nm3
log I(s) 9.99×10-1 9.99×10-2 9.99×10-3 9.99×10-4
Immunoglobulin G subclass 4 small angle scattering data  s, nm-1
ln I(s)
Immunoglobulin G subclass 4 Guinier plot ln 9.99×10-1 Rg: 4.9 nm 0 (4.9 nm)-2 s2
(sRg)2I(s)/I(0)
Immunoglobulin G subclass 4 Kratky plot 1.104 0 √3 sRg
p(r)
Immunoglobulin G subclass 4 pair distance distribution function Rg: 5.0 nm 0 Dmax: 16.3 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Immunoglobulin G subclass 4 CUSTOM IN-HOUSE model
Synchrotron SAXS data from solutions of glycosylated immunoglobulin G4 (IgG4) 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 (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 2.79 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.

The data displayed in this entry are interpolated SAXS profile representations extrapolated to s = 0 and I(0) = 1.

Immunoglobulin G subclass 4 (IgG4)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   145 kDa
Sequence   FASTA