I think the Cl- moves faster and should be the leading ion, then the protein, with negatively charged glycine at the top of the sandwich. Otherwise it explains the SDS-page stacking and resolving gel nicely. Thank you.
But this wouldn't make any sense, if the glycine has a zero net charge but is at the top of the sandwich, there is no force pushing the proteins down into a sandwich. The glycine isn't pulled anywhere due to the zero net charge. In the video's example, the proteins push the glycine which creates resistance as the glycine doesn't move on it's own as the non-charged variant.
@@bobu5213 Glycine has an IP of 5.97, so at pH 6.8 it is negatively charged, not neutral. It's just that the glycine is more frequently in the neutral state and therefore moving slower. Glycine forming a "wall" makes no sense at all UNLESS it is negatively charged and therefore repells the equally negatively charged proteins. What actually happens is that the fast chloride and the slow glycine leave the proteins inbetween in a region of low ion concentration, resulting in them being the only carriers of current, i.e. getting accelerated until they run into the strongly charged chloride front
I have a question. After the sandwich of chlorine ions, proteins, and glycine reaches the resolving gel, the glycine leaves for the positive electrode. Do the Chlorine ions remain in the gel with the traveling proteins, or are they removed by some other process.
Hi there, great video. Do the proteins automatically enter the resolving gel (even without changing the voltage) or do they only enter into the resolving gel the moment the voltage is changed? Thanks!
You stated that glycine and Cl ions are in the buffer. Could this buffer be a Tris buffer? Which product in polyacrylamide gel contains glycine and chlorine?
I think the Cl- moves faster and should be the leading ion, then the protein, with negatively charged glycine at the top of the sandwich. Otherwise it explains the SDS-page stacking and resolving gel nicely. Thank you.
But this wouldn't make any sense, if the glycine has a zero net charge but is at the top of the sandwich, there is no force pushing the proteins down into a sandwich. The glycine isn't pulled anywhere due to the zero net charge. In the video's example, the proteins push the glycine which creates resistance as the glycine doesn't move on it's own as the non-charged variant.
@@bobu5213 Glycine has an IP of 5.97, so at pH 6.8 it is negatively charged, not neutral. It's just that the glycine is more frequently in the neutral state and therefore moving slower. Glycine forming a "wall" makes no sense at all UNLESS it is negatively charged and therefore repells the equally negatively charged proteins. What actually happens is that the fast chloride and the slow glycine leave the proteins inbetween in a region of low ion concentration, resulting in them being the only carriers of current, i.e. getting accelerated until they run into the strongly charged chloride front
I couldn't understand this, you saved me, thank you very much.
Your accent sounds much more Western compared to your previous videos... two thumbs up :)
Wonderful explanation 😊😊
Sir can you please upload starch gel electrophoresis
What's the best percentage of separation and stacking gel for protein around 37 kda?
I have a question. After the sandwich of chlorine ions, proteins, and glycine reaches the resolving gel, the glycine leaves for the positive electrode. Do the Chlorine ions remain in the gel with the traveling proteins, or are they removed by some other process.
Hi there,
great video.
Do the proteins automatically enter the resolving gel (even without changing the voltage) or do they only enter into the resolving gel the moment the voltage is changed?
Thanks!
Great video!
Perfectly explained
You stated that glycine and Cl ions are in the buffer. Could this buffer be a Tris buffer? Which product in polyacrylamide gel contains glycine and chlorine?
Cl from Hcl
Glycine from running buffer
Sir please upload bioreactors
actually, amazing video
Thank you so much!
Thanks
Thank you sir
Thank you
Thank you sir 😊
woooww thank you
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Asmw
Thank you