7. What sort of proteins will bind most tightly to a cation exchange column at a

Question

7. What sort of proteins will bind most tightly to a cation exchange column at a given pH? a. Proteins with a net positive charge at that pH b. Proteins with a net negative charge at that p c. Proteins with a net neutral charge at that pH 8. Which of the following techniques relies on antibodies to recognize a protein of interest? a. Mass spectrometry b. SDS-PAGE with Coomassie blue staining e. Solid phase peptide synthesis d. Western blotting 9. Which of the following things can not be determined by mass spectrometry? Choose one. a. b. c. d. The molecular weight of a protein The relative abundance of a protein The sequence of a protein The subcellular localization of a protein 10. Put the following steps for determining the sequence of an unknown protein by mass spec in order from start to finish. Note that two of these steps will not be used Centrifuge the peptides to separate them by molecular mass. Compare the peptide sequences found against a database of predicted protein sequences to determine which protein they are from Digest the protein into peptides by treating it with proteases like trypsin Reconstruct the sequence of the peptide by looking at the difference in mass of each successive fragment Separate Tag the protein with an affinity tag such as GST Use a mass spectrometer to fragment the peptides and measure the mass of fragment a. b. c. d. the unknown protein using chromatography and gel electrophoresis e. f. g. 11. What size polypeptide chains would most typically be made by solid phase peptide synthesis? a. Chains up to 3 residues long b. Chains up to 30 residues long c. Chains up to 300 residues long d. Chains up to 3000 residues long 12. Fill in the blanks with the phrases "N-terminus" and "C-terminus" to accurately describe the process of peptide synthesis: "The first amino acid of the chain is attached to a solid support via its-terminus. Its -terminus is free to react. When the next amino acid is added, it has a protecting group (FMOC) at terminus and an activating group (DCC) at its -terminus. After the coupling reaction, the FMOC is removed, and the peptide is ready for the addition of the next amino acid Overall, the peptide chain is built up from the -terminus to the -terminus."

Explanation / Answer

7)

b) Proteins with a net negative charge at that pH.

8)

d) Western blotting.

9)

d) The subcellular localization of proteins.

10)  

d)  Reconstruct the sequence of the peptide ny looking at the difference in mass of each successive fragements.

f) Tag the protein with an affinity tag such as GST.

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