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 | |