CHAPTER 4 HOMEWORK PROTEIN STRUCTURE 1. The primary structure of a protein refers to: a) the order in which the amino acids are bonded together in a polypeptide chain. B) the cofactors and other...

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CHAPTER 4 HOMEWORK PROTEIN STRUCTURE 1. The primary structure of a protein refers to: a) the order in which the amino acids are bonded together in a polypeptide chain. B) the cofactors and other prosthetic groups found in the protein c) The folding pattern observed in the protein d) The arrangement of polypeptide chains in the protein, if it has more than one. 2. Peptide bonds cannot rotate. This is because: a) the amino acid side chains are too bulky to allow this. B) Internal hydrogen bonding hinders rotation. C) interaction with water molecules hinders rotation D) the peptide bond has considerable double bond character 3. Polypeptide chains prefer the trans conformation. This is because: a) This distances hydrophilic groups from hydrophobic groups b) this minimizes crowding of side chains c) This brings hydrophilic groups in contact with water molecules d) This allows proteins to fold more easily 4. Ramachandran plots indicate that protein conformation is largely a function of: a) hydrophobicity b) number of amino acids c) torsion angles d) arrangement of prosthetic groups 5. Which of these is a description of secondary structure? A) insulin has 50 amino acids b) Insulin has several alpha helical segments c) insulin has a folded globular structure d) insulin has 2 polypeptide chains 6. Motifs are recognizable patterns of: a) primary structure b) secondary structure c) tertiary structure d) quaternary structure 7. Domains are recognizable patterns of: a) primary structure b) secondary structure c) tertiary structure d) quaternary structure 8. Subunits differ from domains because: a) subunits are connected by peptide bonds while domains are not b) domains are connected by peptide bonds while subunits are not c) domains are larger than subunits d) subunits are larger than domains 9. Beta barrel is a type of: a) subunit b) motif c) domain d) transport protein 10. The major secondary structure seen in collagen is: a) alpha helix b) beta sheet c) collagen helix d) random coil or nonrepetitive 11. The major secondary structure seen in hemoglobin is: a) alpha helix b) beta sheet c) collagen helix d) random coil or nonrepetitive 12. Although all of these play a part in protein folding, the one which contributes the most is: a) salt bridges b) hydrogen bonds c) Van der Waals interactions d) hydrophobic effect 13. An intermediate folding stage seen in protein denaturation or renaturation is called : a) domain b) motif c) subunit d) molten globule 14. Proteins which do not renature spontaneously when denaturation conditions are removed may need the assistance of: a) a prosthetic group b) a higher salt concentration c) a lower temperature d) a chaperone protein 15. The information needed for correct protein folding is encoded in: a) the surrounding molecules b) the protein’s amino acid sequence c) the pH of the aqueous medium d) the electrolyte composition of the aqueous solution