 
			 
			MCQOPTIONS
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				This section includes 17 Mcqs, each offering curated multiple-choice questions to sharpen your Genetic Engineering knowledge and support exam preparation. Choose a topic below to get started.
| 1. | Cyanogen bromide is used for cleavage of junctions. It cleaves after ________ residues. | 
| A. | methionine | 
| B. | tryptophan | 
| C. | cysteine | 
| D. | phenolic acid | 
| Answer» B. tryptophan | |
| 2. | Enterokinase is an intestinal enzyme that converts _______ to ________ | 
| A. | pepsinogen, pepsin | 
| B. | pepsin, pepsinogen | 
| C. | trypsinogen, trypsin | 
| D. | trypsin, trypsinogen | 
| Answer» D. trypsin, trypsinogen | |
| 3. | His tagged proteins can be eluted using EDTA or a pH gradient from the matrix. | 
| A. | True | 
| B. | False | 
| Answer» B. False | |
| 4. | Pel B protein is produced in plants and helps in the degradation of ______ | 
| A. | vacuole | 
| B. | plasma membrane | 
| C. | cell wall | 
| D. | mitochondria | 
| Answer» D. mitochondria | |
| 5. | Glutathione-S-Transferase (GST) enzyme is used for the conjunction of Glutathione molecules and is having a protective function in many organisms. | 
| A. | True | 
| B. | False | 
| Answer» B. False | |
| 6. | A short peptide region fused to a protein of interest is known as ___________ | 
| A. | tag | 
| B. | oligonucleotide | 
| C. | fragment | 
| D. | dimer | 
| Answer» B. oligonucleotide | |
| 7. | There are some advantages of expressing protein as a fusion protein. It may enhance stability, folding ______ and ______ formation. | 
| A. | solubility, phosphodiester bond formation | 
| B. | insolubility, phosphodiester bond formation | 
| C. | solubility, disulphide bond formation | 
| D. | insolubility, disulphidebond formation | 
| Answer» D. insolubility, disulphidebond formation | |
| 8. | CYANOGEN_BROMIDE_IS_USED_FOR_CLEAVAGE_OF_JUNCTIONS._IT_CLEAVES_AFTER__________RESIDUES.?$ | 
| A. | methionine | 
| B. | tryptophan | 
| C. | cysteine | 
| D. | phenolic acid | 
| Answer» B. tryptophan | |
| 9. | Enterokinase is an intestinal enzyme that converts _______ to _______? | 
| A. | pepsinogen, pepsin | 
| B. | pepsin, pepsinogen | 
| C. | trypsinogen, trypsin | 
| D. | trypsin, trypsinogen | 
| Answer» D. trypsin, trypsinogen | |
| 10. | His tagged proteins can be eluted using EDTA or a pH gradient from the matrix. Is the given statement true or false? | 
| A. | True | 
| B. | False | 
| Answer» B. False | |
| 11. | Pel B protein is produced in plants and helps in degradation of ______ | 
| A. | vacuole | 
| B. | plasma membrane | 
| C. | cell wall | 
| D. | mitochondria | 
| Answer» D. mitochondria | |
| 12. | Often, protein to be expressed is fused with histidine and it is called as histidine tags. For their purification, matrix containing ______ is used. | 
| A. | calcium ions | 
| B. | nickel ions | 
| C. | iron ions | 
| D. | fluorine ions | 
| Answer» C. iron ions | |
| 13. | Thioredexin protein contains two _______ residues. | 
| A. | cysteine | 
| B. | cystine | 
| C. | adenine | 
| D. | guanine | 
| Answer» B. cystine | |
| 14. | Maltose binding protein is the product of ______ gene in E.coli and located in ______ | 
| A. | malE, nucleus | 
| B. | malD, nucleus | 
| C. | malE, periplasmic space | 
| D. | malD, periplasmic space | 
| Answer» D. malD, periplasmic space | |
| 15. | Glutathione-S-Transferase (GST) enzyme is used for conjunction of Glutathione molecules and is having a protective function in many organisms. Is the given statement true or false? | 
| A. | True | 
| B. | False | 
| Answer» B. False | |
| 16. | A short peptide region fused to a protein of interest is known as: | 
| A. | tag | 
| B. | oligonucleotide | 
| C. | fragment | 
| D. | dimer | 
| Answer» B. oligonucleotide | |
| 17. | There are some advantages of expressing protein as a fusion protein. It may enhance stability, folding, ______ and ______ formation. | 
| A. | solubility, phosphodiester bond formation | 
| B. | insolubility, phosphodiester bond formation | 
| C. | solubility, disulphide bond formation | 
| D. | insolubility, disulphidebond formation | 
| Answer» D. insolubility, disulphidebond formation | |