Deciphering Copper Coordination in the Mammalian Prion Protein Amyloidogenic Domain

Salzano G, Brennich M, Mancini G, Tran T, Legname G, D’Angelo P, Giachin G, Biophysical Journal (2020) DOI

SASDEW7 – C-terminal truncated bank vole prion protein (amino acids 90-231)

Major prion protein
MWI(0) 16 kDa
MWexpected 16 kDa
VPorod 29 nm3
log I(s) 2.50×101 2.50×100 2.50×10-1 2.50×10-2
Major prion protein small angle scattering data  s, nm-1
ln I(s)
Major prion protein Guinier plot ln 2.51×101 Rg: 2.3 nm 0 (2.3 nm)-2 s2
(sRg)2I(s)/I(0)
Major prion protein Kratky plot 1.104 0 3 sRg
p(r)
Major prion protein pair distance distribution function Rg: 2.4 nm 0 Dmax: 9.4 nm

Data validation


Fits and models


log I(s)
 s, nm-1
C-terminal truncated bank vole prion protein (amino acids 90-231) Rg histogram Rg, nm
Major prion protein EOM/RANCH model

Synchrotron SAXS data from solutions of the C-terminal truncated bank vole prion protein (amino acids 90-231) in 25 mM ammonium acetate, 250 mM NaCl, pH 5.5 were collected using size exclusion chromatography SAXS (SEC-SAXS) 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 = 0.099 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). SEC-SAXS was performed at 20 °C using the following parameters: Column type, Superdex 75 10/300 GL (GE Healthcare); Flow rate: 0.5 mL/min; Total acquisition time: 50 min; Injection concentration: 10 mg/mL; Injection volume: 250 μL. The data obtained through the sample elution peak (1963-2030 1 s frames) were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted and the individual subtracted data sets were scaled and averaged to generate the scattering profile displayed in this entry.

Major prion protein
Mol. type   Protein
Organism   Myodes glareolus
Olig. state   Monomer
Mon. MW   16.1 kDa
 
UniProt   Q8VHV5 (90-231)
Sequence   FASTA