Binding structures of SERF1a with NT17-polyQ peptides of huntingtin exon 1 revealed by SEC-SWAXS, NMR and molecular simulation.

Lin TC, Shih O, Tsai TY, Yeh YQ, Liao KF, Mansel BW, Shiu YJ, Chang CF, Su AC, Chen YR, Jeng US, IUCrJ (2024) Europe PMC

SASDVQ5 – HTT1 peptide

HTT1
MWexperimental 19 kDa
MWexpected 8 kDa
VPorod 18 nm3
log I(s) 2.59×10-2 2.59×10-3 2.59×10-4 2.59×10-5
HTT1 small angle scattering data  s, nm-1
ln I(s)
HTT1 Guinier plot ln 2.60×10-2 Rg: 1.9 nm 0 (1.9 nm)-2 s2
(sRg)2I(s)/I(0)
HTT1 Kratky plot 1.104 0 3 sRg
Dmax: 7 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data from solutions of HTT1 peptide in sodium phosphate buffer, pH 7.4 were collected on the TPS13A beam line at the NSRRC (Hsinchu, Taiwan) using a Eiger X 1M & 9M detector at a sample-detector distance of 2.5 m and at a wavelength of λ = 0.08265 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). Solute concentrations ranging between 4 and 8 mg/ml were measured at 10°C. Three successive 2 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.

The sodium phosphate buffer solution contains 480 μL of 10 mM PB, pH 7.4, 16.5 μL of 100 mM NaOH, and 10 μL of 1% trifluoroacetic acid (TFA).

HTT1
Mol. type   Protein
Organism   synthetic construct
Olig. state   Dimer
Mon. MW   4.0 kDa
Sequence   FASTA