Why would someone want to purify a protein? Select all that apply. To solve Its

Question

Why would someone want to purify a protein? Select all that apply. To solve Its structure via NMR or X-ray crystallography. To predict Its structure using blolnformatles and computer prediction programs. To Identify its enzymatic function by characterizing It In vitro using various assays. To identify its enzymatic function by characterizing it In vitro using various assays. This is the generic name for a biochemical test you would do in the lab (to determine if your protein Is present or active): This type of chromatopraphy. separates proteins based on charge. This type of chromatography separates proteins based on their innate ability to bind specifically to a given molecule. If you purified your protein taking advantage of its high number of arginines and lysines. you likely used: cation exchange chromatography anion exchange chromatography gel filtration affinity chromatography If you purified your protein taking advantage of its ability to bind to ATP, you likely used: cation exchange chromatography anion exchange chromatography gel filtration affinity chromatography If you purified your protein taking advantage of the fact that it is 59 amino adds long, you probably used: cation exchange chromatography anion exchange chromatography gel filtration affinity chromatography

Explanation / Answer

1) Actually, the purification of protein is done then of course we can directly move towards to identify its enzymatic function by characterizing it in vitro using various assays. To predict its structure via NMR, the purified protein can also be further processed to solve.

But as far as purified protein structure prediction using Bioinformatics tools is concerned it would be possible only if the purified protein so obtained could be sequenced suing MS (Mass spectrometry) technique.

2) to determine the presence of Protein we can go for Bradford biochemical test.

3) Isoelectric focusing is a technique which separates the protein based on their charge.

4) Affinity Chromatography

5) Since Lys and Arg are +vely charged residues we should go for anion exchange chromatography.

6)Since the concerned protein is having a binding affinity towards ATP then for its purification, Affinity Chromatography should be followed.

7)Gel filtration is the best way to purify protein made up more residues as mentioned in the Q. 59 amino acid residues.

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