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

SASDKD9 – Mothers against decapentaplegic homolog 4, SMAD4, linker fragment (amino acids 141-271)

Mothers against decapentaplegic homolog 4 (linker)
MWexperimental 18 kDa
MWexpected 14 kDa
VPorod 45 nm3
log I(s) 3.24×101 3.24×100 3.24×10-1 3.24×10-2
Mothers against decapentaplegic homolog 4 (linker) small angle scattering data  s, nm-1
ln I(s)
Mothers against decapentaplegic homolog 4 (linker) Guinier plot ln 3.24×101 Rg: 3.7 nm 0 (3.7 nm)-2 s2
(sRg)2I(s)/I(0)
Mothers against decapentaplegic homolog 4 (linker) Kratky plot 1.104 0 3 sRg
Dmax: 17.5 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of Mothers against decapentaplegic homolog 4, SMAD4, linker fragment (amino acids 141-271) 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). . The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

X-ray wavelength: UNKNOWN. X-ray exposure time: UNKNOWN. Sample detector distance: UNKNOWN. Sample concentration(s): UNKNOWN.

Mothers against decapentaplegic homolog 4 (linker) (SMAD4-linker)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   13.9 kDa
 
UniProt   Q13485 (141-271)
Sequence   FASTA