What does SDS-PAGE accomplish in protein analysis?

SDS-PAGE, which stands for Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis, is a powerful technique used in protein analysis primarily for denaturing proteins. The process involves treating proteins with SDS, a detergent that denatures proteins by binding to them and imparting a negative charge proportional to their length. This denaturation disrupts secondary, tertiary, and quaternary structures, causing proteins to unfold into their primary linear amino acid sequences.

As a result, SDS-PAGE allows for the separation of proteins based on their molecular weight during electrophoresis, where the denatured proteins migrate through a polyacrylamide gel. This separation is essential for analyzing protein size, determining the purity of protein samples, and identifying differences among proteins in a mixture.

While there may be other processes that involve amplifying proteins, determining specific sequences, or combining different protein types, those functions are not achieved through SDS-PAGE. This technique's primary role centers specifically around the denaturation and size separation of proteins.