Discussion
Home ‣ Biochemistry ‣ Structure and Properties of Peptides Comments
- Question
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
- Correct Answer
- hydrophobic residues
- 1. 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
- 2. 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
- 3. 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
- 4. 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 Discuss
- 5. 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
- 6. 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
- 7. An oil drop with a polar coat is a metaphor referring to the three dimensional structure of
Options- A. fibrous proteins
- B. collagen
- C. globular proteins
- D. silk protein Discuss
- 8. What is the proportion of glycine residues in collagenous regions?
Options- A. One-fourth
- B. One-third
- C. Half
- D. One-tenth Discuss
- 9. Secondary structure in protein refers to
Options- A. linear sequence of amino acids joined together by peptide bond
- B. three dimensional arrangement of all amino acids in polypeptide chain
- C. regular folding of regions of the polypeptide chain
- D. protein made up of more than one polypeptide chain Discuss
- 10. What is the effect of a decrease in pH on hemoglobin oxygen affinity?
Options- A. Decrease in oxygen affinity
- B. Increase in oxygen affinity
- C. No effect on oxygen affinity
- D. Increase affinity in muscle cell otherwise decrease Discuss
Structure and Properties of Peptides problems
Search Results
Correct Answer: have Y = F = 180°
Correct Answer: partial double bond
Correct Answer: the iron atom in the heme group
Correct Answer: usually trans unless proline is the next amino acid
Correct Answer: roughly parallel to the helix axis
Correct Answer: phospho-diester bonds
Correct Answer: globular proteins
Correct Answer: One-third
Correct Answer: regular folding of regions of the polypeptide chain
Correct Answer: Decrease in oxygen affinity
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