How does SDS enable the analysis of proteins by SDS-PAGE?
It cleaves the peptide bonds of the protein.
Proteins become coated with a uniform negative charge, giving all proteins a consistent charge-to-mass ratio.
SDS disrupts disulfide bonds.
The hydrophobic tail of SDS binds to the hydrophobic regions of proteins and denatures them.
Options B and C are both correct.
Options B and D are both correct