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Amino Acids, Peptides and Proteins 1. At very low pH most amino acids is have a _____ charge. Ans: positive Link to: 3.1 Difficulty: Easy 2. Disulfide bonds are formed between two ______________________ amino acids. Ans: cysteine Link to: 3.1 Difficulty: Easy 3. In the condensation of two amino acids one molecule of ___________ is lost. Ans: water Link to: 3.2 Difficulty: Easy 4. Amino acids linked together in a chain are called a _____________. Ans: polypeptide Link to: 3.2 Difficulty: Easy 5. Protein in the food we eat is digested by enzymes called ______. Ans: peptidases Link to: 3.2 Difficulty: Easy 6. A deficiency in vitamin C causes defects in collagen, which is classified as a _____ protein. 22 Chapter 3 Ans: structural Link to: 3.3 Difficulty: Easy 7. The protein ______ participates in oxygen dispersal in muscle. Ans: myoglobin Link to: 3.3 Difficulty: Easy 8. A polypeptide can fold into an individual unit of structure called a ______________. Ans: domain Link to: 3.3 Difficulty: Easy 9. A protein that contains more than one subunit is called ______. Ans: oligomeric Link to: 3.4 Difficulty: Easy 10. A secondary structure which forms a coiled shape with a specific repeating pattern, stabilized by hydrogen bonds, is called a(n)________. Ans: alpha helix Link to: 3.4 Difficulty: Medium 11. The sequence of amino acids in a protein, from N to C-terminus, is referred to as the _______ structure. Ans: primary Link to: 3.4 Difficulty: Easy 23 Chapter 3 12. Related proteins contain large regions of sequence ______. Ans: homology Link to: 3.5 Difficulty: Easy 13. The purity and size of a protein can be determined by ________. Ans: electrophoresis Link to: 3.5 Difficulty: easy 14. The amino acid which gives the taste of unami is _______. Ans: glutamic acid Link to: 3.5 Difficulty: Easy 15. Sickle cell anemia is caused by an amino acid ______. Ans: substitution (or replacement) Link to: 3.5 Difficulty: easy 16. The collective group of all the proteins is called the: a) protosome. b) proteome. c) genome. d) prion. e) liposome. Ans: b Link to: Intro Difficulty: Easy 17. Amino acids are considered zwitterions because they: a) exist as dipolar ionic species. 24 Chapter 3 b) were discovered by H. Zwitter. c) are white solids. d) are soluble in water. e) conduct an electric current. Ans: a Link to: 3.1 Difficulty: Easy 18. The pK values for amino groups are typically in the pH range: a) 0-2 b) 4-6 c) 6-8 d) 8-10 e) 4-8 Ans: d Link to: 3.1 Difficulty: Medium 19. Amino acids contain the following groups linked to a carbon: a) an amino group and a carboxylate group. b) an amino group and an R group . c) a carboxylate group and an R group. d) an amino group and a carboxylate group and an R group. e) none of the above Ans: d Link to: 3.1 Difficulty: Medium 20. The amino acids with charged side chains include: a) aspartate, glutamate, lysine and arginine. b) aspartate, glutamate and glycine. c) aspartate, lysine and arginine. d) aspartate, glutamate, lysine, glycine and arginine. e) none of the above 25 Chapter 3 Ans: a Link to: 3.1 Difficulty: Medium 21. The net charge of the peptide Arg-Phe-Gly-Lys-Glu at pH 7 is: a) +2 b) +3 c) -2 d) +1 e) -3 Ans: d Link to: 3.1 Difficulty: Medium 22. Which of the following is not an amino acid inserted into proteins by a “dedicated” tRNA? a) selenocysteine b) proline c) phosphoserine d) glycine e) asparagine Ans: c Link to: 3.1 Difficulty: Medium 23. In order to design a drug that could enter a cell, a scientist might consider how it would interact with a ____ protein located on the cellular membrane. a) defense b) structural c) catalytic d) immune e) transport Ans: e Link to: 3.3 Difficulty: Medium 26 Chapter 3 24. Which of the following characteristics is consistent with the description of a fibrous protein, but not a globular protein? a) water insoluble b) dissolved in biological fluids c) high content of polar amino acids d) low tensile strength e) often function as transport proteins Ans: a Link to: 3.4 Difficulty: Medium 25. The heme found in myoglobin is a: a) domain. b) prosthetic group. c) zinc finger. d) peptide. e) none of the above Ans: b Link to: 3.4 Difficulty: Medium 26. Which of the following is not a type of secondary structure found in proteins? a) sheet b) helix c) random coil d) random turn e) disulfide bond Ans: e Link to: 3.4-3.5 Difficulty: easy 27. If designing a drug that inhibited a large, multisubunit enzyme, it would be important to know how the drug interacted with the: a) primary structure. b) mRNA structure. c) secondary structure. d) tertiary structure. 27 Chapter 3 e) quaternary structure. Ans: e Link to: 3.4 Difficulty: Medium 28. Proteins with charges can be separated by _______ chromatography. a) exclusion b) size c) affinity d) ion exchange e) gel Ans: d Link to 3.5: Difficulty: Medium 29. Protein sequences can be determined by: a) amino acid sequencing of the protein. b) determining the amino acid composition. c) sequencing the DNA of the protein’s corresponding gene. d) a and b e) a and c Ans: e Link to: 3.5 Difficulty: Medium 30. Protein sequence data cannot be used to: a) determine mutations. b) estimate three-dimensional structure. c) determine the exact DNA sequence. d) deduce about biological function. e) obtain evolutionary data. Ans: c Link to: 3.5 Difficulty: Medium 28 Chapter 3 29