An Integrative Structural Biology Analysis of Von Willebrand Factor Binding and Processing by ADAMTS-13 in Solution.

Del Amo-Maestro L, Sagar A, Pompach P, Goulas T, Scavenius C, Ferrero DS, Castrillo-Briceño M, Taulés M, Enghild JJ, Bernadó P, Gomis-Rüth FX, J Mol Biol 433(13):166954 (2021) Europe PMC

SASDKU8 – von Willebrand Factor peptide 6mg/ml

von Willebrand factor
MWexperimental 12 kDa
MWexpected 11 kDa
VPorod 27 nm3
log I(s) 1.92×10-2 1.92×10-3 1.92×10-4 1.92×10-5
von Willebrand factor small angle scattering data  s, nm-1
ln I(s)
von Willebrand factor Guinier plot ln 1.93×10-2 Rg: 3.0 nm 0 (3.0 nm)-2 s2
(sRg)2I(s)/I(0)
von Willebrand factor Kratky plot 1.104 0 √3 sRg
p(r)
von Willebrand factor pair distance distribution function Rg: 3.4 nm 0 Dmax: 14.9 nm

Data validation

Fits and models

log I(s)
 s, nm-1
von Willebrand Factor peptide 6mg/ml Rg histogram Rg, nm
Synchrotron SAXS data from solutions of von Willebrand Factor peptide in 10 mM HEPES, 150 mM NaCl, pH 7.4 were collected on the EMBL P12 beam line at PETRA III (Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.124 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 6.00 mg/ml was measured at 20°C. 40 successive 0.050 second frames were collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

SAXS data for vWF-strep peptide at 6mg/ml

Tags: idp
von Willebrand factor (VWF(1596-1668))
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   11.2 kDa
 
UniProt   P04275 (1596-1668)
Sequence   FASTA