Gel Electrophoresis separates proteins based on size and charge?

Started by rak173
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rak173

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Or by size only since SDS gives negative charge to all proteins, so basically the only thing that matters is the size. I know that DNA is separated based on size and charge.
 
Polyacrylamide gel electrophoresis, called "Native PAGE" or "Nondenaturing PAGE" when SDS is not added, conserves the charge of the proteins and separates them according to their molecular weight-charge ratio. When SDS is added, it linearizes the proteins (destroys their tertiary structure) and coats them with the negatively charged molecule to offset the charge of their individual R groups. This is called SDS-PAGE. This means that SDS-PAGE separates according to their molecular weight. The intention of denaturing is to remove their 3-dimensional shapes that could slow down their progression through the gel (imagine you are comparing a linear protein and a ring protein with a higher surface area) and in this way standardize the proteins' solely on their molecular weight.

Hope this helps!
 
Polyacrylamide gel electrophoresis, called "Native PAGE" or "Nondenaturing PAGE" when SDS is not added, conserves the charge of the proteins and separates them according to their molecular weight-charge ratio. When SDS is added, it linearizes the proteins (destroys their tertiary structure) and coats them with the negatively charged molecule to offset the charge of their individual R groups. This is called SDS-PAGE. This means that SDS-PAGE separates according to their molecular weight. The intention of denaturing is to remove their 3-dimensional shapes that could slow down their progression through the gel (imagine you are comparing a linear protein and a ring protein with a higher surface area) and in this way standardize the proteins' solely on their molecular weight.

Hope this helps!

So SDS-PAGE separates based on Weight only and PAGE alone separates on Charge and Weight both?