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Home ‣ Biochemistry ‣ Structure and Properties of Peptides Comments
- Question
The peptide bond in proteins is
Options- A. only found between proline residues
- B. usually cis unless proline is the next amino acid
- C. usually trans unless proline is the next amino acid
- D. is planar because of steric hinderance
- Correct Answer
- usually trans unless proline is the next amino acid
- 1. Hydrogen bonds in a-helices are
Options- A. more numerous than Vander Waals interactions
- B. not present at Phe residues
- C. analogous to the steps in a spiral staircase
- D. roughly parallel to the helix axis Discuss
- 2. The resonance structures that can be drawn for the peptide bond indicate that the peptide bond
Options- A. is stronger than an ordinary single bond
- B. has partial double bond character
- C. both (a) and (b)
- D. is still not completely understood Discuss
- 3. The peptide bond in proteins is
Options- A. planar, but rotates to three preferred dihedral angles
- B. nonpolar, but rotates to three preferred dihedral angles
- C. nonpolar, and fixed in a trans conformation
- D. planar, and usually found in a trans conformation Discuss
- 4. Which of the following statement is incorrect?
Options- A. Hemoglobin and myoglobin are the two oxygen binding proteins
- B. Hemoglobin transports O2 in the blood
- C. Myoglobin stores O2 in muscles
- D. None of the above Discuss
- 5. The same peptide, Val-Lys-Glu-Met-Ser-Trp-Arg-Ala. was digested with chymotrypsin to produce
Options- A. Val-Lys + Glu-Met-Ser + Trp-Arg-Ala.
- B. Val-Lys-Glu-Met-Ser-Trp + Arg-Ala.
- C. Val-Lys-Glu-Met-Ser + Trp-Arg-Ala.
- D. Val-Lys-Glu-Met + Ser-Trp-Arg-Ala. Discuss
- 6. The oxygen in hemoglobin and myoglobin is bound to
Options- A. the iron atom in the heme group
- B. the nitrogen atoms on the heme
- C. histidine residues in the protein
- D. lysine residues in the protein Discuss
- 7. The nature of peptide bond can be best explained as
Options- A. partial double bond
- B. truly double bond
- C. Hydrogen bond
- D. Van der waals force Discuss
- 8. Peptides in the fully extended chain conformation
Options- A. have Y = F = 180°
- B. do not occur in nature
- C. also have a cis geometry in their peptide bonds
- D. are equivalent to the (3-sheet structure Discuss
- 9. Heme is the binding pocket of myoglobin and hemoglobin and is composed of
Options- A. negatively charged residues
- B. polar residues
- C. hydrophobic residues
- D. positively charged residues Discuss
- 10. The different orders of protein structure are determined by all of the following bond types except
Options- A. peptide bonds
- B. phospho-diester bonds
- C. disulfide bridges
- D. hydrogen bonds Discuss
Structure and Properties of Peptides problems
Search Results
Correct Answer: roughly parallel to the helix axis
Correct Answer: both (a) and (b)
Correct Answer: planar, and usually found in a trans conformation
Correct Answer: None of the above
Correct Answer: Val-Lys-Glu-Met-Ser-Trp + Arg-Ala.
Correct Answer: the iron atom in the heme group
Correct Answer: partial double bond
Correct Answer: have Y = F = 180°
Correct Answer: hydrophobic residues
Correct Answer: phospho-diester bonds
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