Why do all proteins move towards the positive electrode in SDS-PAGE?
why do proteins in SDS-PAGE separate according to molecular mass?
how can SDS-PAGE be tuned to different optimal ranges of molecular mass?
how is the pH gradient established in IEF?
how does the charge of a protein change as it moves in a IEF gel and how does this change affect the drift speed.
To answer this question, read the original publications on DISK-electrophoresis (doi:10.1111/j.1749-6632.1964.tb14207.x) and SDS-PAGE (doi:10.1038/227680a0).
https://www.thermofisher.com/iq/en/home/life-science/protein-biology/protein-biology-learning-center/protein-biology-resource-library/pierce-protein-methods/overview-electrophoresis.html
To find answers to your questions - and more - go to the Learning Center: Foci section in aesociety.org
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