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.
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Sir much obliged from Bangladesh,
I am a first year student of Biochemistry and Molecular biology, Dhaka university
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Sir thank you so much u always save me just before my exams. thank u so much
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Sir my professor makes his lectures from your videos 🙏
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Nice presentation
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Thank you for lecture sir
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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.
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Thank you very much sir 😊
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Sir you haven't explained about resolving and stacking gel ..
That we will discuss in a separate video
Best as always 😍
Thank you
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
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