|
High concentration of ovalbumin solutions (214 mg/ml) was made, and NaOH with the final concentration 0.16 M was added to the ovalbumin solution. The ovalbumin changed into a transparent gel after a couple of minutes. During this process, the ovalbumin proteins experienced a partial unfolding and cross linked to each other. Because the proteins link to form extended materials, the parameters Rg and monomer molecular weight do not apply here. Buffer subtraction was performed with a measurement of 0.9 M NaOH.
Both measurements at small and wide angles were performed at 10°C and the data merged to create a single profile over the range q ∈ [0.08, 10] nm−1.
The small angle sample measurement (1 x 1800 s exposure) was performed using a rotating-anode system with Cu Kα radiation (λ = 0.1542 nm) from a Bruker-Nonius FR591 generator operated at 3.4 kW. Collimation was performed using circular pinholes and Osmic Max-Flux confocal optics. The scattered X-rays (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle) were collected using a Bruker Hi-Star area detector. Data were collected at sample−detector distances of 150 cm. To minimize background, an integral vacuum with a pressure of < 0.3 mbar was maintained along the entire flight path.
The wide angle were performed at the National Synchrotron Light Source (NSLS; Brookhaven, NY, USA). Incident X-ray energy was 8.00 keV (λ = 0.155 nm). These measurements were done in air due to constraints of the sample holder geometry. Each measurement was made at a single sample position with a MAR-CCD detector at the wave vector range of q ∈ [0.8, 10] nm−1.
Concentration max = UNKNOWN
|
|
Ovalbumin
(Ova)
|
| Mol. type |
|
Protein |
| Organism |
|
Gallus gallus |
| Olig. state |
|
Monomer |
| Mon. MW |
|
42.8 kDa |
| |
| UniProt |
|
P01012
|
| Sequence |
|
FASTA |
| |
|
s, nm-1
