Scattering approaches to unravel protein solution behaviors in ionic liquids and deep eutectic solvents: From basic principles to recent developments

Han Q, Veríssimo N, Bryant S, Martin A, Huang Y, Pereira J, Santos-Ebinuma V, Zhai J, Bryant G, Drummond C, Greaves T, Advances in Colloid and Interface Science :103242 (2024) DOI

SASDSP9 – Buffer under-substracted hen egg white lysozyme in 1mol% ethylammonium nitrate

Lysozyme C
MWexperimental 14 kDa
MWexpected 14 kDa
VPorod 23 nm3
log I(s) 9.68×10-3 9.68×10-4 9.68×10-5 9.68×10-6
Lysozyme C small angle scattering data  s, nm-1
ln I(s)
Lysozyme C Guinier plot ln 9.69×10-3 Rg: 1.6 nm 0 (1.6 nm)-2 s2
(sRg)2I(s)/I(0)
Lysozyme C Kratky plot 1.104 0 √3 sRg
p(r)
Lysozyme C pair distance distribution function Rg: 1.6 nm 0 Dmax: 6.2 nm

Data validation

There are no models related to this curve.

Synchrotron SAXS data from solutions of hen egg white lysozyme in 1 mol% ethylammonium nitrate, pH 8 were collected on the SAXS/WAXS beam line at the Australian Synchrotron (Melbourne, Australia) using a Pilatus3 S 2M detector at a sample-detector distance of 2.2 m and at a wavelength of λ = 0.1033 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 5.00 mg/ml was measured at 25°C. 20 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.

Buffer scattering intensities deliberately under-subtracted, by an unknown factor.

Lysozyme C
Mol. type   Protein
Organism   Gallus gallus
Olig. state   Monomer
Mon. MW   14.3 kDa
 
UniProt   P00698 (19-147)
Sequence   FASTA