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

SASDK89 – Mothers against decapentaplegic homolog 2, SMAD2, linker-MH2 fragment (amino acids 186-467) 2.2 mg/ml

Mothers against decapentaplegic homolog 2 (linker-MH2)
MWexperimental 98 kDa
MWexpected 99 kDa
log I(s) 9.64×101 9.64×100 9.64×10-1 9.64×10-2
Mothers against decapentaplegic homolog 2 (linker-MH2) small angle scattering data  s, nm-1
ln I(s)
Mothers against decapentaplegic homolog 2 (linker-MH2) Guinier plot ln 9.64×101 Rg: 4.2 nm 0 (4.2 nm)-2 s2
(sRg)2I(s)/I(0)
Mothers against decapentaplegic homolog 2 (linker-MH2) Kratky plot 1.104 0 3 sRg
Dmax: 19 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Mothers against decapentaplegic homolog 2, SMAD2, linker-MH2 fragment (amino acids 186-467) 2.2 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 2.20 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.

Mothers against decapentaplegic homolog 2 (linker-MH2) (SMAD2 (linker-MH2))
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Other
Mon. MW   33.1 kDa
 
UniProt   Q15796 (186-467)
Sequence   FASTA