Molecular Determinants of Fibrillation in a Viral Amyloidogenic Domain from Combined Biochemical and Biophysical Studies

Nilsson J, Baroudi H, Gondelaud F, Pesce G, Bignon C, Ptchelkine D, Chamieh J, Cottet H, Kajava A, Longhi S, International Journal of Molecular Sciences 24(1):399 (2022) DOI

SASDQC7 – Region within the N-terminal domain of P/V/W protein of Hendra virus (PNT3 region) mutated YYY --> AAA

Non-structural protein V (Y211A, Y212A, Y213A mutant)
MWexperimental 21 kDa
MWexpected 15 kDa
VPorod 49 nm3
log I(s) 2.14×10-2 2.14×10-3 2.14×10-4 2.14×10-5
Non-structural protein V (Y211A, Y212A, Y213A mutant) small angle scattering data  s, nm-1
ln I(s)
Non-structural protein V (Y211A, Y212A, Y213A mutant) Guinier plot ln 2.15×10-2 Rg: 4.0 nm 0 (4.0 nm)-2 s2
(sRg)2I(s)/I(0)
Non-structural protein V (Y211A, Y212A, Y213A mutant) 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 the PNT3 region of P/V/W protein (mutated YYY --> AAA) in 50 mM sodium phosphate, pH 7.2 were collected on the SWING beam line at SOLEIL (Saint-Aubin, France) using a Eiger 4M detector at a sample-detector distance of 2 m and at a wavelength of λ = 0.10332 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A 50.00 μl sample at 5 mg/ml was injected at a 0.30 ml/min flow rate onto a Agilent AdvanceBio SEC 2.7 µm - 130 Å column at 20°C. 810 successive 0.990 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.

Tags: idp
Non-structural protein V (Y211A, Y212A, Y213A mutant) (HeV_PNT3(AAA))
Mol. type   Protein
Organism   Hendra virus (isolate Horse/Autralia/Hendra/1994)
Olig. state   Monomer
Mon. MW   14.9 kDa
 
UniProt   O55777 (200-310)
Sequence   FASTA