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.
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.