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

SASDQF7 – Region within N-terminal domain of P/V/W protein of Nipah virus (PNT3 region)

Non-structural protein V
MWexperimental 21 kDa
MWexpected 15 kDa
VPorod 47 nm3
log I(s) 2.99×10-2 2.99×10-3 2.99×10-4 2.99×10-5
Non-structural protein V small angle scattering data  s, nm-1
ln I(s)
Non-structural protein V Guinier plot ln 3.00×10-2 Rg: 3.7 nm 0 (3.7 nm)-2 s2
(sRg)2I(s)/I(0)
Non-structural protein V Kratky plot 1.104 0 3 sRg
Dmax: 16.5 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 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 (NiV PNT3)
Mol. type   Protein
Organism   Nipah henipavirus
Olig. state   Monomer
Mon. MW   15.0 kDa
 
UniProt   Q997F2 (200-314)
Sequence   FASTA