Visualizing the Effect of pH on Solubilization of the Influenza A Viral Core

Begin with purified influenza A viral core fractions, treated with various pH conditions, ranging from neutral to acidic.
The viral core fraction contains matrix proteins and nucleoproteins.
Heat the samples to denature the proteins.
Load onto a polyacrylamide gradient gel.
Initiate electrophoresis to separate the proteins based on molecular weight, forming distinct bands.
Incubate the gel in a fixation solution to immobilize the proteins.
Wash to remove fixative, add colloidal Coomassie dye, and incubate. The dye binds to proteins, allowing visualization of the bands.
Remove the dye and wash to destain the gel, which enhances band visibility.
Capture a high-resolution image of the gel.
At neutral pH, the higher intensity of the matrix protein and nucleoprotein bands indicates that the viral core remains intact and retains associated proteins.
As pH decreases, band intensity progressively diminishes.
This indicates that acidic conditions trigger viral core disassembly and promote protein solubilization during purification.

To carry out SDS-PAGE, heat all the samples at 95 degrees Celsius for 10 minutes. Load 20 microliters of the dissolved pellets onto a precast gradient Bis-Tris mini-gel and