Conformational Disorder Analysis of the Conditionally Disordered Protein CP12 from Arabidopsis thaliana in Its Different Redox States

Del Giudice A, Gurrieri L, Galantini L, Fanti S, Trost P, Sparla F, Fermani S, International Journal of Molecular Sciences 24(11):9308 (2023) DOI

SASDSM2 – AtCP12-2 in an oxidized form

CP12-2 (D77G)
MWI(0) 10 kDa
MWexpected 8 kDa
VPorod 10 nm3
log I(s) 9.76×100 9.76×10-1 9.76×10-2 9.76×10-3
CP12-2 (D77G) small angle scattering data  s, nm-1
ln I(s)
CP12-2 (D77G) Guinier plot ln 9.77×100 Rg: 2.0 nm 0 (2.0 nm)-2 s2
(sRg)2I(s)/I(0)
CP12-2 (D77G) Kratky plot 1.104 0 3 sRg
p(r)
CP12-2 (D77G) pair distance distribution function Rg: 2.3 nm 0 Dmax: 9 nm

Data validation


Fits and models


log I(s)
 s, nm-1
AtCP12-2 in an oxidized form Rg histogram Rg, nm
CP12-2 (D77G) EOM/RANCH model
CP12-2 (D77G) EOM/RANCH model

Synchrotron SAXS data from solutions of AtCP12-2 in an oxidized form in 25 mM potassium phosphate, pH 7.5 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a sample-detector distance of 2.9 m and at a wavelength of λ = 0.09919 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 0.3 and 5.4 mg/ml were measured at 4°C. 10 successive 1 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. The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.

CP12-2 (D77G) (AtCP12)
Mol. type   Protein
Organism   Arabidopsis thaliana
Olig. state   Monomer
Mon. MW   8.3 kDa
 
UniProt   A0A178VHQ2 (54-131)
Sequence   FASTA