Conformational landscape of multidomain SMAD proteins

Gomes T, Martin-Malpartida P, Ruiz L, Aragón E, Cordeiro T, Macias M, Computational and Structural Biotechnology Journal (2021) DOI

SASDK29 – Mothers against decapentaplegic homolog 2, SMAD2, wild-type 1.3 mg/ml

Mothers against decapentaplegic homolog 2
MWexperimental 66 kDa
MWexpected 160 kDa
log I(s) 6.97×101 6.97×100 6.97×10-1 6.97×10-2
Mothers against decapentaplegic homolog 2 small angle scattering data  s, nm-1
ln I(s)
Mothers against decapentaplegic homolog 2 Guinier plot ln 6.98×101 Rg: 3.8 nm 0 (3.8 nm)-2 s2
(sRg)2I(s)/I(0)
Mothers against decapentaplegic homolog 2 Kratky plot 1.104 0 3 sRg
Dmax: 21 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Mothers against decapentaplegic homolog 2, SMAD2, wild-type 1.3 mg/ml in 20 mM Tris, 150 mM NaCl, pH 7.2 were collected on the BM29 beam line at the ESRF storage ring (Grenoble, France) using a Pilatus 1M detector (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 1.30 mg/ml was measured at 10°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Protein in a concentration-dependent monomer-dimer-timer equilibrium. X-ray wavelength: UNKNOWN. X-ray exposure time: UNKNOWN. Sample detector distance: UNKNOWN. CAUTION! Guinier region severely truncated. PED: https://proteinensemble.org/PED00197, https://proteinensemble.org/PED00198, https://proteinensemble.org/PED00199

Tags: idp PED
Mothers against decapentaplegic homolog 2 (SMAD2)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Other
Mon. MW   53.3 kDa
 
UniProt   Q15796 (1-467)
Sequence   FASTA