The C-terminal region of the human p23 chaperone modulates its structure and function.

Seraphim TV, Gava LM, Mokry DZ, Cagliari TC, Barbosa LR, Ramos CH, Borges JC, Arch Biochem Biophys 565:57-67 (2015) Europe PMC

SASDBK6 – Truncated construct of human p23 (1-131)

Prostaglandin E synthase 3 (1-131)
MWexperimental 18 kDa
MWexpected 16 kDa
VPorod 31 nm3
log I(s) 1.63×10-2 1.63×10-3 1.63×10-4 1.63×10-5
Prostaglandin E synthase 3 (1-131) small angle scattering data  s, nm-1
ln I(s)
Prostaglandin E synthase 3 (1-131) Guinier plot ln 1.63×10-2 Rg: 1.9 nm 0 (1.9 nm)-2 s2
(sRg)2I(s)/I(0)
Prostaglandin E synthase 3 (1-131) Kratky plot 1.104 0 √3 sRg
p(r)
Prostaglandin E synthase 3 (1-131) pair distance distribution function Rg: 1.9 nm 0 Dmax: 7 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of truncated human p23 (1-131) in 25 mM Tris-HCl, 100 mM NaCl, 5 mM β-mercaptoethanol, pH 7.5 were collected on the SAXS1 Beamline at the Brazilian Synchrotron Light Laboratory (Campinas, Brazil) using a 20Hz Pilatus 300K detector at a sample-detector distance of 1 m and at a wavelength of λ = 0.1488 nm (I(s) vs s, where s = 4π sin θ/λ and 2θ is the scattering angle). Solute concentrations ranging between 1 and 2 mg/ml were measured at 20°C. Two successive 30 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.

Samples were measured at 1 mg/mL and 2 mg/mL in 1 mm path-length mica cells. All curves were inspected for X-ray damage and aggregation. The experimental molecular weight was determined by analytical ultracentrifugation.

Prostaglandin E synthase 3 (1-131) (PTGES, Sba1, p23)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   15.7 kDa
 
UniProt   Q15185 (1-131)
Sequence   FASTA