MCQOPTIONS
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MCQOPTIONS
This section includes 15 Mcqs, each offering curated multiple-choice questions to sharpen your Protein Engineering knowledge and support exam preparation. Choose a topic below to get started.
| 1. |
Helix capping is the phenomenon in which, the side chains of which two flanking residues fold back to form hydrogen bonds with one of the four-terminal residues of the helix? |
| A. | Pro, Val |
| B. | Gly, Val |
| C. | Val, Ile |
| D. | Asn, Gln |
| Answer» E. | |
| 2. |
Which disease is caused by the regular ingestion of the seeds from the sweet pea? |
| A. | Scurvy |
| B. | Diabetes |
| C. | AIDS |
| D. | Lathyrism |
| Answer» E. | |
| 3. |
Which disease results from the dietary deficiency of vitamin C? |
| A. | Jaundice |
| B. | Malaria |
| C. | Cancer |
| D. | Scurvy |
| Answer» E. | |
| 4. |
Which is the most abundant protein in all vertebrates? |
| A. | Keratin |
| B. | Tapasin |
| C. | Connexin |
| D. | Collagen |
| Answer» E. | |
| 5. |
Which among the following are the principal component of the outer layer of the skin (epidermis) and its related appendages, such as hair, horn, nails, and feathers? |
| A. | Calrectin |
| B. | Connexin |
| C. | Collagen |
| D. | Keratin |
| Answer» E. | |
| 6. |
Parallel beta-sheets are more stable than antiparallel beta-sheets. |
| A. | True |
| B. | False |
| Answer» C. | |
| 7. |
Regular secondary structures such as alpha-helices or the strands of beta-sheets are often connected by a stretch of a polypeptide that changes direction abruptly. What are these structures? |
| A. | Incomplete sheets |
| B. | Inverse helix |
| C. | Small helix |
| D. | Turns or beta-bends |
| Answer» E. | |
| 8. |
Beta-sheets are sometimes also called as pleated sheets . |
| A. | False |
| B. | True |
| Answer» C. | |
| 9. |
The peptide C=O bond of the nth residue of the backbone of alpha-helix points along and forms a hydrogen bond with the peptide N H group of which among the following residue? |
| A. | (n+1)<sup>th</sup> |
| B. | (n+2)<sup>th</sup> |
| C. | (n+3)<sup>th</sup> |
| D. | (n+4)<sup>th</sup> |
| Answer» E. | |
| 10. |
What are the pitch length of alpha-helix and the number of residues per turn? |
| A. | 5.3 Armstrong, 6.4 residues |
| B. | 3.4 Armstrong, 5.6 residues |
| C. | 3.6 Armstrong, 5.4 residues |
| D. | 5.4 Armstrong, 3.6 residues |
| Answer» E. | |
| 11. |
The alpha-helix is a right-handed helix. |
| A. | False |
| B. | True |
| Answer» C. | |
| 12. |
Who discovered the alpha-helix structure in a protein molecule? |
| A. | Lynn Margulis |
| B. | Francis Collins |
| C. | Louis Pasteur |
| D. | Linus Pauling |
| Answer» E. | |
| 13. |
What are the most common regular secondary structures found in proteins? |
| A. | Alpha-helix and turns |
| B. | Beta-sheets and loops |
| C. | Loops and turns |
| D. | Alpha-helix and beta-sheets |
| Answer» E. | |
| 14. |
The peptide group in a protein has a rigid, planar structure. Which interactions give the peptide bond its partial double bond character? |
| A. | Covalent |
| B. | Non-covalent |
| C. | Hydrophobic |
| D. | Resonance |
| Answer» E. | |
| 15. |
Which among the following structure represents the local spatial arrangement of a polypeptide without regard to the conformation of its side chains? |
| A. | Primary structure |
| B. | Tertiary structure |
| C. | Quaternary structure |
| D. | Secondary structure |
| Answer» E. | |