What do proteins that are larger or electrically neutral do in a polyacrylamide gel during electrophoresis?

In the context of polyacrylamide gel electrophoresis, larger proteins experience more resistance as they navigate through the gel matrix, which is composed of many small pores. Since these proteins have to push their way through the network of polymer chains in the gel, they move more slowly compared to smaller proteins that can more easily maneuver through the spaces between the gel matrix.

Furthermore, electrically neutral proteins are not influenced by the electric field that drives the migration of charged proteins, so they do not exhibit any net movement towards either electrode. As a result, larger, electrically neutral proteins tend to have a diminished migration rate, which is why they are observed to move slower through the gel during electrophoresis.