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

SASDNL6 – Retinoblastoma protein at 2 mg/ml

Retinoblastoma-associated protein
MWexperimental 44 kDa
MWexpected 41 kDa
VPorod 64 nm3
log I(s) 5.84×10-2 5.84×10-3 5.84×10-4 5.84×10-5
Retinoblastoma-associated protein small angle scattering data  s, nm-1
ln I(s)
Retinoblastoma-associated protein Guinier plot ln 5.84×10-2 Rg: 2.5 nm 0 (2.5 nm)-2 s2
(sRg)2I(s)/I(0)
Retinoblastoma-associated protein Kratky plot 1.104 0 3 sRg
Dmax: 7.9 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of retinoblastoma protein in 20 mM sodium phosphate pH 7.0, 200 mM NaCl, 1mM DTT, pH 7 were collected on the EMBL P12 beam line at PETRA III (DESY, Hamburg, Germany) using a Pilatus 6M detector at a sample-detector distance of 3 m and at a wavelength of λ = 0.1244 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 2.00 mg/ml was measured at 25°C. 20 successive 0.045 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.

Retinoblastoma-associated protein (Rb)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   41.2 kDa
Sequence   FASTA