What happens to proteins during PAGE in terms of their state?

During Polyacrylamide Gel Electrophoresis (PAGE), proteins typically undergo denaturation. This process involves unfolding the proteins, which allows them to be separated based on their size as they migrate through the gel matrix. Denaturation is crucial for achieving the desired resolution and separation since it minimizes interactions that would otherwise keep the proteins in their native, functional states.

Maintaining proteins in their native state during PAGE could lead to issues in separation because the natural conformation of the proteins may promote aggregation or complex formation. Hydrolysis of proteins does not occur in this context, as PAGE focuses on separation rather than breaking down the polypeptide chains. Additionally, while some proteins may become insoluble under certain conditions, the primary purpose of PAGE is to analyze soluble proteins in a denatured form, allowing for effective size-based separation.