SDS-PAGE creates conditions for separating proteins by an identifying characteristic, molecular weight. In this simulation, you will learn how SDS, the acrylamide gel, buffer solutions, and the electric current work together to separate proteins.

Running an SDS-PAGE

In this lab, students will determine if a particular sized protein is present in their samples. To do this, they must learn about the mechanisms of how SDS-PAGE works including deciding on which gel size to use, how the sample buffer prepares the sample, how to assemble the electrophoresis chamber, and ultimately the interactions between pH, the buffer solutions, and the electric current.

Mechanisms behind SDS-PAGE

In order to determine if the sample contains a protein of a specific molecular weight, students first need to select the right acrylamide gel concentration. This simulation allows them to trial different concentrations to see the effect on protein separation. From here, they prepare the sample through visualizing the effects of each component of the sample buffer on the sample itself. They will then run an SDS-PAGE by assembling the electrophoresis chamber and learning how the current and ions of the buffer solutions interact. With the results of the SDS-PAGE being ready immediately, students will determine which samples contain the target protein. 

Gel Review

With SDS-PAGE thoroughly explored, students will evaluate their stained gel to identify if the samples have evidence of the target protein. They will also evaluate other gels as usable or unusable and identify reasons that may have caused the outcome. 

By understanding SDS-PAGE, will you find the target protein and be able to identify a successful gel?