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

SASDKH9 – Mothers against decapentaplegic homolog 4, SMAD4, MH1 fragment (amino acids 10-140)

Mothers against decapentaplegic homolog 4 (MH1 fragment)
MWexperimental 10 kDa
MWexpected 15 kDa
VPorod 24 nm3
log I(s) 1.28×101 1.28×100 1.28×10-1 1.28×10-2
Mothers against decapentaplegic homolog 4 (MH1 fragment) small angle scattering data  s, nm-1
ln I(s)
Mothers against decapentaplegic homolog 4 (MH1 fragment) Guinier plot ln 1.28×101 Rg: 1.6 nm 0 (1.6 nm)-2 s2
(sRg)2I(s)/I(0)
Mothers against decapentaplegic homolog 4 (MH1 fragment) Kratky plot 1.104 0 √3 sRg
Dmax: 6 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of Mothers against decapentaplegic homolog 4, SMAD4, MH1 fragment (amino acids 10-140) 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). 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. Sample concentration(s): UNKNOWN.

Mothers against decapentaplegic homolog 4 (MH1 fragment) (SMAD4 (MH1))
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   15.2 kDa
 
UniProt   Q13485 (10-140)
Sequence   FASTA