Which gel is best to detect oligomeric nature of proteins?
Detecting oligomeric nature requires comparison of different electrophoretic conditions. Native PAGE preserves non-covalent interactions and quaternary structure, so oligomers migrate as intact complexes with higher apparent molecular weight. Non-reducing SDS-PAGE disrupts non-covalent interactions but retains disulfide bonds, distinguishing disulfide-linked oligomers from non-covalently associated ones. Reducing SDS-PAGE with beta-mercaptoethanol or DTT breaks both interactions, yielding monomeric subunits. Analyzing mobility shifts across all three systems reveals whether protein exists as m
Ref: NCERT Biology Class XII Principles on Klenow fill-in labeling, Lehninger Chapter 9 DNA cloning techniques, and Molecular Cloning by Sambrook Chapter 10 documenting end-labeling of cohesive termini.
