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

SASDK59 – Mothers against decapentaplegic homolog 2, SMAD2, linker fragment (amino acids 175-262)

Mothers against decapentaplegic homolog 2 (linker)
MWexperimental 11 kDa
MWexpected 10 kDa
VPorod 20 nm3
log I(s) 1.08×101 1.08×100 1.08×10-1 1.08×10-2
Mothers against decapentaplegic homolog 2 (linker) small angle scattering data  s, nm-1
ln I(s)
Mothers against decapentaplegic homolog 2 (linker) Guinier plot ln 1.09×101 Rg: 2.9 nm 0 (2.9 nm)-2 s2
(sRg)2I(s)/I(0)
Mothers against decapentaplegic homolog 2 (linker) Kratky plot 1.104 0 3 sRg
Dmax: 14 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Mothers against decapentaplegic homolog 2, SMAD2, linker fragment (amino acids 175-262) 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). Solute concentrations ranging between 1 and 4.5 mg/ml were 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. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

X-ray wavelength: UNKNOWN. X-ray exposure time: UNKNOWN. Sample detector distance: UNKNOWN.

Mothers against decapentaplegic homolog 2 (linker) (SMAD2-linker)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   9.7 kDa
 
UniProt   Q15796 (175-262)
Sequence   FASTA