SDS-PAGE (Sodium Dodecyl Sulfate - Polyacrylamide Gel Electrophoresis)
separates proteins according to their primary structure of size but not amino acid sequence.
Properties of SDS-PAGE
Acrylamide pore size depends on concentration.
Small proteins travel quickly through pores.
Mobility is proportional to log(MW) (Molecular Weight)
Sodium Dodecyl Sulfate (SDS) disrupts non-covalent interactions, thus gives proteins a negative charge.
Beta-Mercaptoethanol disrupts disulphide bonds.
Quanternary Structure is H2L2 where H2 (High MW) and L2 (Low MW)