Conformational buffering underlies functional selection in intrinsically disordered protein regions.

González-Foutel NS, Glavina J, Borcherds WM, Safranchik M, Barrera-Vilarmau S, Sagar A, Estaña A, Barozet A, Garrone NA, Fernandez-Ballester G, Blanes-Mira C, Sánchez IE, de Prat-Gay G, Cortés J, Bernadó P, Pappu RV, Holehouse AS, Daughdrill GW, Chemes LB, Nat Struct Mol Biol (2022) Europe PMC

SASDNQ6 – Early E1A protein at 7.0 mg/ml

Early E1A protein
MWexperimental 17 kDa
MWexpected 13 kDa
log I(s) 6.82×10-2 6.82×10-3 6.82×10-4 6.82×10-5
Early E1A protein small angle scattering data  s, nm-1
ln I(s)
Early E1A protein Guinier plot ln 6.82×10-2 Rg: 4.1 nm 0 (4.1 nm)-2 s2
(sRg)2I(s)/I(0)
Early E1A protein Kratky plot 1.104 0 √3 sRg

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of early E1A protein in 20 mM sodium phosphate pH 7.0, 200 mM NaCl, 1mM DTT, pH 7 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 = 0.1033 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 7.00 mg/ml was measured at 10°C. 40 successive 0.900 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.

Early E1A protein (E1A)
Mol. type   Protein
Organism   Human adenovirus C serotype 5
Olig. state   Monomer
Mon. MW   12.7 kDa
Sequence   FASTA