Different buffers are used in gel electrophoresis to create different conditions for protein separation. The choice of buffer depends on the type of gel electrophoresis being performed, such as native or denaturing, and the type of protein being analyzed. The buffer affects the pH, ionic strength, and other chemical properties of the gel, which can impact the resolution of proteins. For example, the Tris-glycine buffer system is widely used because it creates a stacking effect that produces sharp protein bands, while the Laemmli system can cause band distortion or loss of resolution due to its highly alkaline operating pH. Therefore, the choice of buffer can significantly affect the resolution of proteins in gel electrophoresis.

https://www.thermofisher.com/iq/en/home/life-science/protein-biology/protein-biology-learning-center/protein-biology-resource-library/pierce-protein-methods/overview-electrophoresis.html

In gel electrophoresis, the choice of buffer can significantly influence the resolution of proteins on the gel. The buffer composition affects several factors, such as pH, conductivity, and buffering capacity, which in turn impact the movement and separation of proteins during electrophoresis.

In the paper you mentioned, the comparison between Tricine-Tris and Glycine-Tris buffers highlights the differences in resolution. Tricine is a zwitterionic buffer with a lower pKa value compared to glycine. Here are a few factors that contribute to the improved resolution with Tricine-Tris compared to Glycine-Tris:

These video playlists might be helpful to you:

https://www.youtube.com/playlist?list=PLzBiAPKi8vOPbE7Db9mKwloe34E8rXXEU

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Thanks a lot to everybody. Your answers were really helpful.

Best,

David