Do Proteins With Smaller Relative Molecular Mass Migrate Faster in SDS-Polyacrylamide Gel Electrophoresis
SDS-PAGE employs an electric field to separate proteins based on their migration through a polyacrylamide gel matrix. SDS (sodium dodecyl sulfate) is an anionic surfactant that binds uniformly to proteins, denaturing them and imparting a consistent negative charge. As a result, protein migration becomes independent of their native charge and is primarily determined by their size (molecular mass).
In SDS-PAGE, the migration rate of proteins is chiefly governed by their molecular mass. Proteins with smaller relative molecular mass migrate more rapidly than those with larger mass, as they can traverse the gel matrix more easily. In contrast, larger proteins experience greater resistance due to their size, resulting in slower movement through the gel pores.
MtoZ Biolabs, an integrated chromatography and mass spectrometry (MS) services provider.
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