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

SASDNV6 – Early E1A protein, SEC-SAXS data

Early E1A protein
MWexperimental 16 kDa
MWexpected 13 kDa
VPorod 45 nm3
log I(s) 1.23×10-2 1.23×10-3 1.23×10-4 1.23×10-5
Early E1A protein small angle scattering data  s, nm-1
ln I(s)
Early E1A protein Guinier plot ln 1.24×10-2 Rg: 3.6 nm 0 (3.6 nm)-2 s2
(sRg)2I(s)/I(0)
Early E1A protein Kratky plot 1.104 0 3 sRg
Dmax: 17.5 nm

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). 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 0.50 ml/min flow rate onto a GE Superdex 200 5/150 column 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