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Electrophoretic separation at pH 6 of a sample of polypeptide 1 (mw 100) polypeptide 2 (mw 200) and polypeptide 3 (mw 400) would result in which of the following?
(Note: the isoelectric point of each polypeptide occurs at pH 6)
  • a)
    Polypeptide 1 would move the farthest
  • b)
    Polypeptide 2 would move the farthest
  • c)
    Polypeptide 3 would move the farthest
  • d)
    None of the polypeptides would move
Correct answer is option 'D'. Can you explain this answer?
Verified Answer
Electrophoretic separation at pH 6 of a sample of polypeptide 1 (mw 10...
  • The isoelectric point for a polypeptide is the pH at which the molecule does not have a net charge.
  • Electrophoretic separation depends on the existence of a negative net charge.
  • None of the polypeptides would move at pH 6.
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Most Upvoted Answer
Electrophoretic separation at pH 6 of a sample of polypeptide 1 (mw 10...
- **Explanation:**
- **Isoelectric Point (pI):** The isoelectric point (pI) is the pH at which a molecule carries no net electrical charge. At this pH, the molecule will not migrate in an electric field during electrophoresis. For polypeptides, the pI is typically around the average of the pKa values of its constituent amino acids.
- **Electrophoretic Separation:** In electrophoretic separation, molecules migrate towards the electrode of opposite charge based on their net charge. At a pH above the pI of a molecule, it will carry a net negative charge and migrate towards the positive electrode. At a pH below the pI, it will carry a net positive charge and migrate towards the negative electrode.
- **Given Scenario:** In this scenario, the electrophoretic separation is carried out at pH 6, which is the isoelectric point for all three polypeptides (pI = 6). At pH 6, all three polypeptides will have no net charge and will not migrate in the electric field.
- **Conclusion:** Therefore, none of the polypeptides (Polypeptide 1, Polypeptide 2, and Polypeptide 3) would move during electrophoretic separation at pH 6. This is because their charges are balanced at pH 6, resulting in no net migration in the electric field.
- **Answer:** Option D - None of the polypeptides would move
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Electrophoretic separation at pH 6 of a sample of polypeptide 1 (mw 10...
  • The isoelectric point for a polypeptide is the pH at which the molecule does not have a net charge.
  • Electrophoretic separation depends on the existence of a negative net charge.
  • None of the polypeptides would move at pH 6.
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Electrophoretic separation at pH 6 of a sample of polypeptide 1 (mw 100) polypeptide 2 (mw 200) and polypeptide 3 (mw 400) would result in which of the following?(Note: the isoelectric point of each polypeptide occurs at pH 6)a)Polypeptide 1 would move the farthestb)Polypeptide 2 would move the farthestc)Polypeptide 3 would move the farthestd)None of the polypeptides would moveCorrect answer is option 'D'. Can you explain this answer? for MCAT 2025 is part of MCAT preparation. The Question and answers have been prepared according to the MCAT exam syllabus. Information about Electrophoretic separation at pH 6 of a sample of polypeptide 1 (mw 100) polypeptide 2 (mw 200) and polypeptide 3 (mw 400) would result in which of the following?(Note: the isoelectric point of each polypeptide occurs at pH 6)a)Polypeptide 1 would move the farthestb)Polypeptide 2 would move the farthestc)Polypeptide 3 would move the farthestd)None of the polypeptides would moveCorrect answer is option 'D'. Can you explain this answer? covers all topics & solutions for MCAT 2025 Exam. Find important definitions, questions, meanings, examples, exercises and tests below for Electrophoretic separation at pH 6 of a sample of polypeptide 1 (mw 100) polypeptide 2 (mw 200) and polypeptide 3 (mw 400) would result in which of the following?(Note: the isoelectric point of each polypeptide occurs at pH 6)a)Polypeptide 1 would move the farthestb)Polypeptide 2 would move the farthestc)Polypeptide 3 would move the farthestd)None of the polypeptides would moveCorrect answer is option 'D'. Can you explain this answer?.
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