Wow, I'd imagine the SDS anion aggregate of larger proteins would be enough to repulse them at a greater distance than the smaller ones. Funny how a deeper understanding of biophysics contradicts that statement, suggesting the exact opposite. Thanks for such great lectures! You're better than Khan! :)
Your videos are amazing!! Thank you so much for explaining things in such a clear and concise way to aid my professor's explanations. Finally feel like I understand things!
I love your videos ! Please come teach in Trois-Rivieres, Canada, my teacher is the head of the biomed department of my uni and he's so confusing. He talks about his researches and stuff in class but all we want is to know the basics first ! My uni is all in French (my first language, sorry if I made mistakes), but we would certainly like to make the extra effort to be taught in English if you were our teacher !
What books do you refer sir??? Your explanations are way too easy n understandable... You are our saviour... Thank you so much. Pls post lectures on BIOINFORMATICS, if it's possible for you sir
A great video, but tell me: When there is in the end no force that accelerates the proteins, because the forces cancel out each other, how do the proteins still move? I can not imagine the main reason to be is them having enough cinetic energy from the short period of time before they entered the matrix and the friction was not that much of a resistance, because you can interrupt the process, then start it again and the bands will start moving once more. Sorry for my bad english.
Great, minor one is V should be proportional to the Charges/size, this make proteins similar in this respect. Ony differ in the friciton that is also proportiona to the lengthor weight of the protein
