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Sarah_4925
#1 Posted : Saturday, July 18, 2020 8:40:11 PM
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Hello,
In the AAMC Section Bank for Bio/Biochem,in passage 3 question 20 it asks about the conditions that the gel electrophoresis should be performed for a protein. The answer is C)native, and description says, "Use of a denaturing agent will disrupt the interactions between monomers. Use of a reducing agent only will disrupt any disulfide bonds." However in the CC for Biochemistry on page 121 in class we annotated that the SDS-page would require a denaturing deturgent of the protein prior to running it on the gel, which confuses me as it seems to contradict what the AAMC question explains. Would you be able to clarify this as I think I am misunderstanding something.
Thank you very much!
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INSTR_Katerina_102
#2 Posted : Saturday, July 18, 2020 8:55:45 PM
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Hi Sarah,

Could you post the full question for context? This is pretty dependent on what you want to do.

It is true that conventional SDS-PAGE runs denatured proteins on a gel because molecular conformation can affect how something runs, but there are also variants of SDS-PAGE that will look at native variants of proteins - and when you use one or the other is dependant on the situation.

My guess is that maybe you're looking at monomer vs dimer formation of a pair of proteins, and in this case if you denatured and broke apart the dimer, you wouldn't be able to distinguish a sample containing only monomer from a sample containing two monomers in a dimer, but I'd have to look at the full question to be sure.

Hope this helps!

Katt
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