Albumin in patients with liver disease shows an altered conformation.

Paar M, Fengler VH, Rosenberg DJ, Krebs A, Stauber RE, Oettl K, Hammel M, Commun Biol 4(1):731 (2021) Europe PMC

SASDL54 – Human Albumin (P1)

Albumin
MWexperimental 69 kDa
MWexpected 69 kDa
log I(s) 2.92×103 2.92×102 2.92×101 2.92×100
Albumin small angle scattering data  s, nm-1
ln I(s)
Albumin Guinier plot ln 2.92×103 Rg: 2.9 nm 0 (2.9 nm)-2 s2
(sRg)2I(s)/I(0)
Albumin Kratky plot 1.104 0 √3 sRg
p(r)
Albumin pair distance distribution function Rg: 2.9 nm 0 Dmax: 9.3 nm

Data validation

Fits and models

log I(s)
 s, nm-1
Albumin SREFLEX model
Synchrotron SAXS data from solutions of Human Albumin (P1) in 20 mM Tris, 150 mM KCl, 2% glycerol, pH 7.4 were collected on the 12.3.1 (SIBYLS) beam line at the Advanced Light Source (ALS) storage ring (Berkeley, CA, USA) using a Pilatus3 X 2M detector at a sample-detector distance of 2.1 m and at a wavelength of λ = 0.1127 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 55.00 μl sample at 3 mg/ml was injected at a 0.50 ml/min flow rate onto a Shodex KW-800 series column at 20°C. 600 successive 3 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.

Albumin
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   69.4 kDa
 
UniProt   P02768
Sequence   FASTA