Which one of the following purification techniques would most likely be used as

Question

Which one of the following purification techniques would most likely be used as a step in the purification of a protein that will later be used for an activity assay? SDS-PAGE Anion exchange chromatography with diethylaminoethyl cellulose resin Gel filtration chromatography with Superdex-200 resin 2D gel electorphoresis Question 9 2 pts Which of the following statements is not true? Disulfde bridges between Cys residues in the same polypeptide chain can be broken with a reducing agent such as dithiothreitol. Mass spectrometry often allows the identification of a protein without the need for sequencing by comparing the masses of oligopeptides after protein digestion to a database of known oligopeptide masses. Cyanogen bromide cleaves methionine on the amino (N) side of the residue. Trypsin generally cleaves after basic residues. Question 10 Which of the following dissociation constants represents the strongest protein-ligand interaction? Kd 0.3 mM Kd 0.5 nM Kd 500 HM Kd 600 pM

Explanation / Answer

8. The correct answer is SDS-PAGE.

For proteins, SDS-PAGE is usually the first choice as an assay of purity as it is highly reliable and easy. Proteins are seperated based on size and it is highly useful.

9. The third option is incorrect.

Cyanogen Bromide cleaves at the C-end of peptide.

10. The first option is the correct one.

The lower the constant, the stronger is the binding in biological systems.

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