1. Protein purification refers to the
a) Purification of proteins
b) Separation of proteins from other biomolecules
c) Separation of a particular protein from other contaminating proteins
d) all of these
2. Protein separation techniques are often based on the following properties except
a) solubility of the protein
b) viscosity of the protein
c) charge of protein
d) specific binding affinity of the protein
3. Primary steps in protein purification includes
a) Homogenization
b) Differential centrifugation
c) Solubilisation
d) all of these
4. Which of the following detergent is commonly used to release integral proteins from its membranes?
a) urea
b) dimethyl sulphoxide
c) triton X 100
d) cyanogen bromide
5. Salting out process involves
a) precipitation of proteins using ammonium sulphate
b) precipitation of proteins using copper sulphate
c) precipitation of proteins using sodium chloride
d) none of these
6. Which of the following separation method is suited for a protein sample with large differences in molecular mass
a) dialysis
b) salting out process
c) density gradient centrifugation
d) rate zonal centrifugation
7. In which of the following separation method where proteins are separated on the basis of their net charge
a) Affinity chromatography
b) Ion exchange chromatography
c) dialysis
d) gel filtration chromatography
8. In gel filtration chromatography, separation of proteins are based on their
a) size and net charge
b) size and shape
c) size and specific affinity
d) shape and net charge
9. The use of insulin hormone to purify its receptor is an example of
a) Ion exchange chromatography
b) Affinity chromatography
c) Gel filtration chromatography
d) Ligand mediated chromatography
10. In anion exchange chromatography,
a) the column contains negatively charged beads where positively charged proteins bind
b) the column contains positively charged beads where negatively charged proteins bind
c) the column contains both positive and negatively charged beads where proteins bind depending on their net charge
d) all of these
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1. c) Separation of a particular protein from other contaminating proteins
2. b) viscosity of the protein
3. d) all of these
4. c) triton X 100
5. a) precipitation of proteins using ammonium sulphate
6. d) rate zonal centrifugation
7. b) Ion exchange chromatography
8. b) size and shape
9. b) Affinity chromatography
10. b) the column contains positively charged beads where negatively charged proteins bind
a) Purification of proteins
b) Separation of proteins from other biomolecules
c) Separation of a particular protein from other contaminating proteins
d) all of these
2. Protein separation techniques are often based on the following properties except
a) solubility of the protein
b) viscosity of the protein
c) charge of protein
d) specific binding affinity of the protein
3. Primary steps in protein purification includes
a) Homogenization
b) Differential centrifugation
c) Solubilisation
d) all of these
4. Which of the following detergent is commonly used to release integral proteins from its membranes?
a) urea
b) dimethyl sulphoxide
c) triton X 100
d) cyanogen bromide
5. Salting out process involves
a) precipitation of proteins using ammonium sulphate
b) precipitation of proteins using copper sulphate
c) precipitation of proteins using sodium chloride
d) none of these
6. Which of the following separation method is suited for a protein sample with large differences in molecular mass
a) dialysis
b) salting out process
c) density gradient centrifugation
d) rate zonal centrifugation
7. In which of the following separation method where proteins are separated on the basis of their net charge
a) Affinity chromatography
b) Ion exchange chromatography
c) dialysis
d) gel filtration chromatography
8. In gel filtration chromatography, separation of proteins are based on their
a) size and net charge
b) size and shape
c) size and specific affinity
d) shape and net charge
9. The use of insulin hormone to purify its receptor is an example of
a) Ion exchange chromatography
b) Affinity chromatography
c) Gel filtration chromatography
d) Ligand mediated chromatography
10. In anion exchange chromatography,
a) the column contains negatively charged beads where positively charged proteins bind
b) the column contains positively charged beads where negatively charged proteins bind
c) the column contains both positive and negatively charged beads where proteins bind depending on their net charge
d) all of these
Learn more:
- Multiple Choice Questions on Proteins
- Multiple Choice Questions on Protein Structure
- GRE Questions on Proteins
- Biochemistry Practice Test on Amino acids and Proteins
- Multiple Choice Questions on Protein Purification Methods
1. c) Separation of a particular protein from other contaminating proteins
2. b) viscosity of the protein
3. d) all of these
4. c) triton X 100
5. a) precipitation of proteins using ammonium sulphate
6. d) rate zonal centrifugation
7. b) Ion exchange chromatography
8. b) size and shape
9. b) Affinity chromatography
10. b) the column contains positively charged beads where negatively charged proteins bind
Tags:
biochemistry multiple choice
mcq on protein
MCQon Protein Purification
Multiple Choice on Protein Purification
