How Does pH Affect Peptide Separation in Electrophoresis?

In summary, the question is asking about the best option for pH in electrophoresis separation of two peptides with isoelectric points of 10.3 and 7 respectively. The given options are pH 3, 8, or 10. The person asking the question is unsure of how to manage the sign of the charges in order to achieve the best separation. They are wondering if having both peptides with the same charge or opposite charges would be more beneficial.
  • #1
Melow
1
0
Hi all, I have a question about this exercise:

Which is the best option of pH for electrophoresis separation of two peptides with isoelectric points of 10.3 and 7 respectively? The given options of pH are 3,8 or 10.

I've thought that if pH is more than 7, then, there will be positive charge for the peptide of 10.3 pI, and negative charge for the peptide of 7 pI, but i don't know how to manage th sign of the charges to get the best eletrophoresis separation. Is it better to have both of them with the same charge or the opposite charge?

<Moved to homework section. No template>
 
Last edited by a moderator:
Physics news on Phys.org
  • #2
How does the sign of the charge influence how the peptides migrate during electrophoresis?
 

Related to How Does pH Affect Peptide Separation in Electrophoresis?

What is electrophoresis of peptides?

Electrophoresis of peptides is a laboratory technique used to separate and analyze peptides based on their size and charge differences. It involves applying an electric field to a gel matrix, causing the peptides to migrate towards the positive or negative electrode depending on their charge.

Why is electrophoresis of peptides important in scientific research?

Electrophoresis of peptides allows scientists to study and identify specific peptides in a sample, providing valuable information about the protein composition of a sample. It is commonly used in protein structure analysis, drug discovery, and biomarker identification.

What types of electrophoresis techniques are commonly used for peptides?

The most commonly used electrophoresis techniques for peptides are SDS-PAGE (sodium dodecyl sulfate polyacrylamide gel electrophoresis) and capillary electrophoresis. SDS-PAGE is used for separating peptides based on size, while capillary electrophoresis is used for separating peptides based on charge.

What are the limitations of electrophoresis of peptides?

One limitation of electrophoresis of peptides is that it only provides information about the size and charge of the peptides. It does not provide information about the identity of the peptides, which may require additional techniques such as mass spectrometry. Additionally, electrophoresis may not be suitable for all types of peptides, as some may not migrate well in the gel matrix.

How can I optimize my electrophoresis of peptides experiment?

To optimize your electrophoresis of peptides experiment, it is important to carefully choose the appropriate gel matrix, buffer system, and voltage. It is also crucial to handle the peptides carefully to prevent degradation or contamination. Additionally, running a control sample and properly analyzing the results can help ensure the accuracy and reproducibility of the experiment.

Similar threads

How Does Charge Density Affect Electric Field Strength Between Two Cables?
    • Advanced Physics Homework Help
Replies
4
Views
8K
How Does Cis-Platin Affect DNA Replication?
    • Chemistry
Replies
2
Views
2K
How to list arXiv papers on NSF final report
    • STEM Academic Advising
Replies
4
Views
2K
Mathematica This Week's Finds in Mathematical Physics (Week 253)
    • MATLAB, Maple, Mathematica, LaTeX
Replies
20
Views
4K
Mathematica This Week's Finds in Mathematical Physics (Week 241)
    • MATLAB, Maple, Mathematica, LaTeX
Replies
8
Views
3K

Hot Threads

Recent Insights

Back
Top