1. Which of the following protein purification techniques is properly paired wit
ID: 537176 • Letter: 1
Question
1. Which of the following protein purification techniques is properly paired with its description?
A) Fractionation: sodium dodecyl sulfate is used to fractionate proteins based on differences in their solubility as a function of salt concentration.
B) Gel-filtration chromatography: separates proteins on the basis of size. Smaller molecules elute first and the larger molecules elute last.
C) SDS-polyacrylamide gel electrophoresis: separates molecules based on molecular weight. The smallest molecules migrate fastest and as a result are located more toward the bottom of the gel relative to larger molecules.
D) Cation exchange: separates molecules based on overall charge. The least positive molecules elute from the column first and the most positive molecules elute from the column last. The elution order is the result of the positively charged resin molecules of the matrix.
2. Assume the peptide from question 5 is placed in an electrophoresis apparatus similar to the one shown on page 6 of the Chapter 3 summary notes. Which direction would this peptide migrate at pH 7?
options:
At pH 7, the peptide will not migrate.
At pH 7, the peptide will travel to the positive electrode.
At pH 7, the peptide will travel to the negative electrode.
At pH 7, this peptide will degrade into free amino acids.
Thank you!
A)At pH 7, the peptide will not migrate.
B)At pH 7, the peptide will travel to the positive electrode.
C)At pH 7, the peptide will travel to the negative electrode.
D)At pH 7, this peptide will degrade into free amino acids.
Explanation / Answer
1]
Answer is A
B - small molecules elute last
C - based on charge
D - most positive elute first
2]
IF it has overall negative charge it will travel to positive electrode
If it has overall positive charge it will travel to negative electrode
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