Internal nanosecond dynamics in the intrinsically disordered myelin basic protein.

Stadler AM, Stingaciu L, Radulescu A, Holderer O, Monkenbusch M, Biehl R, Richter D, J Am Chem Soc 136(19):6987-94 (2014) Europe PMC

SASDDF6 – Myelin basic protein

Myelin basic protein
MWI(0) 20 kDa
MWexpected 18 kDa
log I(s) 2.04×101 2.04×100 2.04×10-1 2.04×10-2
Myelin basic protein small angle scattering data  s, nm-1
ln I(s)
Myelin basic protein Guinier plot ln 2.05×101 Rg: 3.3 nm 0 (3.3 nm)-2 s2
(sRg)2I(s)/I(0)
Myelin basic protein Kratky plot 1.104 0 3 sRg
p(r)
Myelin basic protein pair distance distribution function Rg: 3.5 nm 0 Dmax: 11.1 nm

Data validation


Fits and models


log I(s)
 s, nm-1
Myelin basic protein Rg histogram Rg, nm
Myelin basic protein EOM/RANCH model
Myelin basic protein EOM/RANCH model
Myelin basic protein EOM/RANCH model
Myelin basic protein EOM/RANCH model
Myelin basic protein EOM/RANCH model
Myelin basic protein EOM/RANCH model

Synchrotron SAXS data from solutions of myelin basic protein in 20 mM NaH2PO4/Na2HPO4, 99.9% v/v D2O, pH 4.8 were collected on the BM29 beam line at the ESRF (Grenoble, France) using a Pilatus 1M detector at a wavelength of λ = 0.099 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). 10 successive 2 second frames were collected at 10°C from a sample at 4.5 mg/ml. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Tags: idp
Myelin basic protein
Mol. type   Protein
Organism   Bos taurus
Olig. state   Monomer
Mon. MW   18.3 kDa
 
UniProt   P02687
Sequence   FASTA