Human Dystrophin Structural Changes upon Binding to Anionic Membrane Lipids.

Dos Santos Morais R, Delalande O, Pérez J, Mias-Lucquin D, Lagarrigue M, Martel A, Molza AE, Chéron A, Raguénès-Nicol C, Chenuel T, Bondon A, Appavou MS, Le Rumeur E, Combet S, Hubert JF, Biophys J 115(7):1231-1239 (2018) Europe PMC

SASDDL9 – Conformation of R1-3 human dystrophin fragment in interaction with anionic phospholipid bicelles (SANS)

R1-3 human dystrophin fragment
MWexperimental 46 kDa
MWexpected 39 kDa
VPorod 100 nm3
log I(s) 1.75×10-1 1.75×10-2 1.75×10-3 1.75×10-4
R1-3 human dystrophin fragment small angle scattering data  s, nm-1
ln I(s)
R1-3 human dystrophin fragment Guinier plot ln 1.75×10-1 Rg: 6.2 nm 0 (6.2 nm)-2 s2
(sRg)2I(s)/I(0)
R1-3 human dystrophin fragment Kratky plot 1.104 0 √3 sRg
p(r)
R1-3 human dystrophin fragment pair distance distribution function Rg: 6.1 nm 0 Dmax: 24.8 nm

Data validation

Fits and models

log I(s)
 s, nm-1
R1-3 human dystrophin fragment YASARA model
SANS data from solutions of the R1-3 human dystrophin fragment with anionic phospholipid bicelles in 20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% v/v D2O, pD 7.5 (pH 7.1) were collected on the D22 SANS instrument at the Institut Laue-Langevin (ILL, Grenoble, France) using a 3He multidetector 128 linear sensitive Reuter-Stokes detector detector at two sample-detector distances a neutron wavelength of λ = 0.6 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 4.20 mg/ml was measured at 22°C at both sample-detector distances as were appropriate solvent blanks prior to data reduction and merging.

The sample-to-detector distance (collimation distance) and exposure times used were: 1.4 m (2.8m), 5 min and; 8m (8 m), 20 min. The CRYSON ill.res file is included in the full entry zip archive.

R1-3 human dystrophin fragment (R1-3)
Mol. type   Protein
Organism   Homo sapiens
Olig. state   Monomer
Mon. MW   38.5 kDa
 
UniProt   P11532 (338-668)
Sequence   FASTA