Design of intrinsically disordered protein variants with diverse structural properties

Pesce F, Bremer A, Tesei G, Hopkins J, Grace C, Mittag T, Lindorff-Larsen K, Science Advances 10(35) (2024) DOI

SASDTJ2 – Low complexity domain of hnRNPA1 (Heterogeneous nuclear ribonucleoprotein A1)

Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1
MWexperimental 15 kDa
MWexpected 13 kDa
VPorod 19 nm3
log I(s) 1.77×10-3 1.77×10-4 1.77×10-5 1.77×10-6
Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 small angle scattering data  s, nm-1
ln I(s)
Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 Guinier plot ln 1.78×10-3 Rg: 2.4 nm 0 (2.4 nm)-2 s2
(sRg)2I(s)/I(0)
Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 Kratky plot 1.104 0 3 sRg
p(r)
Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 pair distance distribution function Rg: 2.5 nm 0 Dmax: 8 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of the low complexity domain of hnRNPA1 in 20 mM HEPES, 150 mM NaCl, 2 mM DTT, pH 7 were collected on the BioCAT 18ID beam line at the Advanced Photon Source (APS), Argonne National Laboratory (Lemont, IL, USA) using a Eiger2 XE 9M (Dectris) detector at a sample-detector distance of 3.7 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 250.00 μl sample at 2.6 mg/ml was injected at a 0.60 ml/min flow rate onto a GE Superdex 75 Increase 10/300 column at 25°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Number of frames = UNKNOWN

Isoform A1-A of Heterogeneous nuclear ribonucleoprotein A1 (hnRNPA1-LCD)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   13.1 kDa
 
UniProt   P09651-2 (186-320)
Sequence   FASTA