How Does pH Affect Peptide Separation in Electrophoresis?

Click For Summary
The optimal pH for electrophoresis separation of two peptides with isoelectric points (pI) of 10.3 and 7 is crucial for effective migration. At a pH above 10.3, the peptide with a pI of 10.3 will carry a positive charge, while the peptide with a pI of 7 will be negatively charged at pH 8 or 10. This charge difference enhances separation, as oppositely charged peptides migrate towards their respective electrodes. Maintaining a pH that ensures the peptides have opposite charges is essential for achieving the best separation during electrophoresis. Understanding the relationship between pH and peptide charge is key to optimizing electrophoretic techniques.
Melow
Messages
1
Reaction score
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
How does the sign of the charge influence how the peptides migrate during electrophoresis?
 

Similar threads

How Does Charge Density Affect Electric Field Strength Between Two Cables?
  • · Replies 3 ·
Replies
3
Views
8K
How Does Cis-Platin Affect DNA Replication?
  • · Replies 2 ·
Replies
2
Views
2K
How to list arXiv papers on NSF final report
  • · Replies 3 ·
Replies
3
Views
3K
Mathematica This Week's Finds in Mathematical Physics (Week 253)
  • · Replies 20 ·
Replies
20
Views
5K
Mathematica This Week's Finds in Mathematical Physics (Week 241)
  • · Replies 8 ·
Replies
8
Views
5K