SDS PAGE gel electrophoresis | sds page principle explained | poly acrylamide gel electrophoresis
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- เผยแพร่เมื่อ 7 ก.พ. 2025
- SDS PAGE gel electrophoresis | sds page principle explained - This lecture explains about SDS PAGE gel electrophoresis principle and SDS PAGE gel electrophoresis procedure in Hindi. Stay tuned to know the following -
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In this video, we'll be discussing the sds page principle, and how it's used to identify and describe molecules. We'll also be discussing the different uses of the sds page, and how it can be helpful in your research.
If you're looking to learn more about the sds page principle, or to understand its uses more fully, then this video is for you! By the end of this video, you'll have a better understanding of this important molecular tool, and will be able to use it to your advantage in your research.
In this video, we'll explore the SDS Page Gels Principle. By understanding the underlying principles of SDS Page Gel Electrophoresis, you'll be able to optimize your results and understand your data more clearly.
SDS Page Gels are one of the most commonly used methods in molecular biology. By understanding the principle behind SDS Page Gel Electrophoresis, you'll be able to get better results from your experiments and make better informed decisions about your data. Watch this video to learn more about the SDS Page Gels Principle and how it can help you in your research.
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Thank you for watching the lecture on SDS PAGE gel electrophoresis principle and procedure.
Sir I found your channel during my undergrad .It was recommended by our professors and I just want to say that It seems I found a treasure ❤
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Sir much obliged from Bangladesh,
I am a first year student of Biochemistry and Molecular biology, Dhaka university
All the best
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Many people do. Helping teachers since a decade
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Thank you so much for appreciating my efforts
Sir thank you so much u always save me just before my exams. thank u so much
You're welcome. Glad to hear that you're getting benefit from my lectures
Best as always 😍
Thank you
Thank you sir❤
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Thanks sir.u make it so easy ..
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Hlo Sir.
Your lectures are very useful to us. I got more knowledge from your's only sir.
Thanking you.
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Thank you sir, very helpful🙏🙏
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Thank you for lecture sir
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Nice presentation
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Thanks
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@@shomusbiologyofficial sir can you make a video about bicarbonate buffer system.
Thank you very much Sir
Most welcome
Thank you sir for this detailed explanation. I just had one query . Sir as the interaction between SDS and amino acids is that there is one SDS between two amino acids. Now, as SDS gives the negative charge, shorter polypeptides or proteins having low molecular weight will be less negatively charged, as they've less number of amino acids . In this case the lengthier polypeptides have more negative charge ..so in that case they should migrate faster towards the anode . Sir, does this parameter exert any influence in the separation process ....🙏
In SDS-PAGE, the movement of proteins is primarily based on their size, not their charge. SDS denatures the proteins and binds to them, giving all proteins a negative charge and essentially neutralizing any charge-based differences between proteins. Therefore, the speed at which a protein moves through the gel is primarily determined by its size, with smaller proteins moving faster and larger proteins moving more slowly. This is why the technique is used to separate proteins based on their molecular weight.
In SDS-PAGE, while it's true that larger proteins will have more SDS bound to them, resulting in a greater negative charge per protein molecule, the overall effect is that the charge-to-mass ratio becomes relatively constant for all proteins. This is because the mass of the protein also increases as it gets larger. As a result, the mobility of the proteins through the gel primarily depends on their size, not on their net charge.
So, larger proteins will indeed have more negative charge, but they also have a larger mass, which balances out the effect on mobility. Therefore, in SDS-PAGE, smaller proteins typically migrate faster through the gel because they encounter less resistance, while larger proteins migrate more slowly due to their greater size.
@@avanimirchandani8190 Thank you so much ... 🙇🌸
@@Bank-al-habib-biometric-soluti Thank you so much 🙇🌸
Sir you haven't explained about resolving and stacking gel ..
That we will discuss in a separate video
Sir when gel formation two type of phase stacking and separating....
very helpful video.
Sir, can you make a video of how to solve part-C question from this topic? would be really helpful🙏
Okay sure
why protein have di-sulphate linkage ? pls
explain it? enybody
CERTAIN AMINOACID HAVE S PRESENT IN THEIR STRUCTURE WHICH MAKES S-S LINKAGE
Sir I need real time pcr
Please I have an exam😢
Already present in my channel
So for lipoproteins will have the same mechanism of action ?
Thank you very much sir 😊
You're welcome