TEST I. Choose the best answer 1. Which is not true about the peptide bond? a. There is free rotation around the peptide bond. b. The peptide pond is planar. c. The peptide bond is formed by elimination of water between two amino acids. d. The peptide bond is the basis of protein structure. 2. The order in which amino acids are linked in peptides/proteins is a. Called the secondary structure of the peptide/protein b. From the Cterminal to the Nterminal end c. From the Nterminal to the Cterminal end d. In alphabetical order 3. Which of the following statements concerning protein structure is not true? a. The primary structure of a protein describes the unique sequence of amino acids in the protein chain. b. Secondary structure describes the peptide bonds joining the amino acids together in the protein chain. c. Tertiary structure describes the overall three dimensional shape of a protein. d. Hydrogen bonding, disulfide bonds, salt bridges, and van der Waals forces are responsible for maintaining the tertiary structure of a protein. 4. In a protein’s tertiary structure, the threonine side chain can participate in a. Electrostatic interaction b. Hydrogen bond c. Disulfide bond d. Hydrophobic interaction 5. Which structural protein is found in bone, tendon, and skin? a. Collagen b. Fibrinogen c. Albumin d. Keratin 6. Tuftsin is a peptide that stimulates and promotes the destruction of tumor cells. Its primary structure is TKPR. Which of the following is not a valid interpretation of its primary structure? a. It is a tetrapeptide. b. Threonine is the Nterminal amino acid and arginine is the Cterminal amino acid. c. The carboxyl group of lysine is joined to the amino group of proline. d. The amino group of arginine is not joined to any other amino acid. 7. What is meant by the “tertiary structure” of a protein?
a. It refers to the peptide bonds that join the amino acids together in the protein chain. b. It describes the regular, repeating structures found in the protein chain. c. It describes the overall three dimensional shape of a protein. d. It describes the association of two or more polypeptide chains to form one functioning protein unit. 8. Hemoglobin and glycoproteins are two examples of proteins that contain a prosthetic group. What is a prosthetic group? a. A nonprotein group bonded to a protein to create a functional unit. b. An inhibitor of the function of the protein. c. A side chain amino acid that is not one of the 20 standard amino acids. d. An artificial amino acid that has been synthesized in the laboratory. 9. What term describes the type of βpleated sheet in which both peptides are aligned form amino terminus to carboxy terminus? a. Antiparellel b. Perpendicular c. Parallel d. Congruent 10. It is called a helix breaker a. G b. P c. F d. W 11. What type of attractive force is responsible for maintaining the secondary structure of a protein? a. Hydrogen bonds between the carbonyl and amine groups of peptide bonds b. Van der Waals forces between the hydrophobic R groups of nonpolar amino acids c. Salt bridges d. SS bonds between thiolcontaining amino acids 12. When a protein undergoes hydrolysis, which of the following things occur? a. Peptide bonds are broken, and individual amino acids are released b. The protein folds into its functional threedimensional shape c. Water adds across each double bond that is present to give an alcohol d. New amino acids are joined to the growing protein chain 13. Which does not belong to the group? a. Casein b. Albumin c. Hemoglobin d. Keratin
14. Denaturation of a protein results in the loss of its native conformation and its biological activity. Which of the following best describes what happens when a protein is denatured? a. The primary structure of the protein is altered b. Peptide bonds are broken and individual amino acids are released c. Secondary, tertiary, and quaternary levels of structure are disrupted d. The Nterminal and Cterminal ends of the protein are hydrolyzed 15. The protein collagen a. Has a double helical structure b. Contains glycine c. Is an example of globular protein d. Is a storage protein 16. Chymotrypsin cleaves proteins selectively at a. K and N b. K and R c. W and Y d. F and T
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