The role of hydration in protein stability: comparison of the cold and heat unfolded states of Yfh1.

Adrover M, Martorell G, Martin SR, Urosev D, Konarev PV, Svergun DI, Daura X, Temussi P, Pastore A, J Mol Biol 417(5):413-24 (2012) Europe PMC

SASDLM5 – frataxin homolog, Yfh1, at 20 °C

Frataxin homolog, mitochondrial
MWI(0) 15 kDa
MWexpected 14 kDa
log I(s) 1.20×10-1 1.20×10-2 1.20×10-3 1.20×10-4
Frataxin homolog, mitochondrial small angle scattering data  s, nm-1
ln I(s)
Frataxin homolog, mitochondrial Guinier plot ln 1.21×10-1 Rg: 2.1 nm 0 (2.1 nm)-2 s2
(sRg)2I(s)/I(0)
Frataxin homolog, mitochondrial Kratky plot 1.104 0 √3 sRg

Data validation

Fits and models

log I(s)
 s, nm-1
frataxin homolog, Yfh1, at 20 °C Rg histogram Rg, nm
Frataxin homolog, mitochondrial EOM/RANCH model
Frataxin homolog, mitochondrial EOM/RANCH model
Frataxin homolog, mitochondrial EOM/RANCH model
Frataxin homolog, mitochondrial EOM/RANCH model
Frataxin homolog, mitochondrial EOM/RANCH model
Synchrotron SAXS data from solutions of frataxin homolog, Yfh1, at 20 °C in 20 mM HEPES, pH 7 were collected on the EMBL X33 beam line at DORIS III (DESY, Hamburg, Germany) using a MAR 345 Image Plate detector at a sample-detector distance of 2.7 m and at a wavelength of λ = 0.154 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. One 120 second frame was collected. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Tags: idp X33
Frataxin homolog, mitochondrial (Frataxin homolog)
Mol. type   Protein
Organism   Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Olig. state   Monomer
Mon. MW   13.8 kDa
 
UniProt   Q07540 (52-174)
Sequence   FASTA