Different types of SDS

[sarmatrac]

This is my understanding of SDS so far:

Nonreducing SDS affects the tertiary structure of a protein but does not affect disulfide bonds.

Reducing SDS page is denaturing and breaks the disulfide bonds. Would you say that this is the most "broken down" a protein can get with SDS techniques?

Are "non-native" SDS techniques a general term for reducing and nonreducing SDS? What is "native" SDS vs "non-native?"

Sorry if this is an obvious question, my book didn't have much on this.

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[aldol16]

Non-reducing SDS also affects secondary structure. It disrupts H-bonding and thus disrupts secondary structure as well. You don't want your proteins to be migrating based on alpha helical and beta sheet content because the latter is more extended and would presumably migrate slower, independently of weight and charge.

Reducing SDS is, for MCAT purposes, the most denatured you can make a protein without actually digesting it.

Native PAGE is letting a protein migrate based on its overall shape and intrinsic charge. No SDS is added so the protein is neither covered in negative charge nor denatured.