NUTR 1st Edition by McGuire - Test Bank

NUTR 1st Edition by McGuire – Test Bank

 

Instant Download – Complete Test Bank With Answers

 

 

Sample Questions Are Posted Below

 

Chapter 5 – Protein

 

True/False

 

1. Protein-rich food sources include meats, fish, nuts, and beans.
2. A protein’s shape depends on its amino acid sequence.
3. Denaturation disrupts a protein’s three-dimensional shape, and therefore causes the protein to lose its function.
4. Chemical digestion of proteins begins in the mouth.
5. Whole proteins can be absorbed through a healthy intestine.
6. Amino acids can be used for ATP production.
7. When dietary protein consumption exceeds protein needs, the extra amino acids can be converted to fat and stored.
8. The human body can recycle and reuse most of its amino acids from disassembled proteins through protein turnover.
9. The American College of Sports Medicine states that athletes require more dietary protein than non-athletes.
10. At-risk groups for protein-energy malnutrition include people with cancer or severe burns and alcoholics.

 

Multiple Choice: Fact Recall Based

 

 

1. The three common components of all amino acids are: a central carbon atom bonded to a hydrogen atom, a carboxylic acid group, and
2. a common side-chain group.
3. a sulfur-containing amino group.
4. a nitrogen-containing amino group.
5. a positively charged R-group.

 

2. Essential amino acids are defined as
3. those that cannot be made by the body in the amounts required and therefore must be consumed in the diet.
4. those that are difficult to find in a well-balanced diet and must be consumed as supplements.
5. those whose nitrogen-containing amino groups must be added in the liver.
6. those required for the synthesis of a limited number of essential proteins.

 

3. Nonessential amino acids
4. are not recycled by the body.
5. can be synthesized from other compounds in the body.
6. are used to synthesize nonessential proteins.
7. all have the same side-chain group.

 

4. The process of transamination
5. is used to synthesize nonessential amino acids.
6. is the process of transferring an amino group from an α-keto acid to an essential amino acid.
7. is the process of transferring an amino group from a nonessential amino acid to an essential amino acid.
8. is the process of transferring an amino group from an essential amino acid to a nonessential amino acid.

 

5. Foods supplying low amounts of one or more essential amino acids are called
6. incomplete protein sources.
7. complementary protein sources.
8. limiting foods.
9. nonessential foods.

 

6. The three steps involved in the process of protein synthesis are cell signaling, transcription, and
7. transamination.
8. deamination.
9. translation.
10. peptide bond cleavage.

 

7. Transcription is
8. the process by which messenger RNA is constructed using DNA as a template.
9. the process of messenger RNA carrying the DNA information out of the nucleus.
10. the process by which a gene is directly converted into a protein.
11. the process by which messenger RNA is directly converted into a protein.

 

8. A gene is
9. a section of DNA that is only used in reproduction.
10. a section of DNA that contains the information necessary to produce a particular protein.
11. a section of DNA that is converted to transfer RNA.
12. a section of DNA that moves outside the nucleus when protein synthesis is required.

 

9. Translation is the process
10. by which messenger RNA leaves the nucleus.
11. by which amino acids are joined using peptide bonds.
12. by which messenger RNA is constructed using DNA as a template.
13. of protein folding.

 

10. The primary structure of a protein is
11. the final structure of the protein.
12. the linear arrangement of amino acids in a single peptide chain.
13. determined by cell signaling events.
14. altered during protein folding.
15. Disruption of protein folding by mechanical shaking, heat, detergents, or acids is called
16. denaturation.
17. transamination.
18. translation.
19. refolding.

 

12. One of the first events that occurs in the stomach in response to the presence of food is the release of _____, a hormone that stimulates the stomach to produce gastric juices.
13. cholecystokinin
14. gastrin
15. secretin
16. insulin

 

13. Pepsinogen is an example of a proenzyme. This means it is
14. an inactive form an enzyme.
15. an enzyme needed for protein digestion.
16. a protease.
17. an enzyme that leads the way for a different enzyme to have activity.

 

14. HCl is important for protein digestion for two reasons: 1) it denatures proteins in the stomach, and 2)
15. it stimulates gastrin release from the stomach.
16. it converts pepsinogen into pepsin.
17. it converts pepsin into pepsinogen.
18. it maintains the acid environment necessary in the small intestine for protein digestion.

 

15. The hormones released by cells in the small intestine in response to the arrival of amino acids and smaller peptides are secretin and cholecystokinin. Together, these hormones stimulate
16. the production of hydrochloric acid and pepsinogen in the stomach.
17. the release of active enzymes from the pancreas.
18. the release of bicarbonate and proenzymes from the pancreas.
19. the release of di- and tripeptides from the absorptive cells that line the small intestine.

 

16. The role of bicarbonate released from the pancreas is to
17. neutralize the acid from the stomach.
18. convert pepsinogen to pepsin.
19. activate the proenzymes released from absorptive cells lining the small intestine.
20. act as a protease.

 

17. The most common food allergies are caused by proteins present in eggs, milk, soy, wheat, and
18. peanuts.
19. walnuts.
20. brazil nuts.
21. coconuts.

 

18. Secretin, gastrin, insulin, and glucagon are examples of proteins that are
19. enzymes.
20. hormones.
21. antibodies.
22. neurotransmitters.

 

19. Protein turnover is
20. the coordinated and continual process of breaking down and resynthesizing proteins.
21. the 3-dimensional rotation of proteins within cells.
22. the breakdown of proteins with subsequent destruction of amino acids.
23. the continual synthesis of proteins following excretion of nonfunctional proteins.

 

20. When nitrogen loss exceeds intake the body is in
21. nitrogen balance.
22. negative nitrogen balance.
23. positive nitrogen balance.

 

21. When nitrogen intake exceeds loss the body is in
22. nitrogen balance.
23. negative nitrogen balance.
24. positive nitrogen balance.

 

22. Because they do not consume any animal products, vegans must make extra efforts to include nutrients that are found in animal products but to a much lesser degree, if at all, in plant products. These nutrients are iron, calcium, zinc, and
23. vitamin B₁₂.
24. vitamin C.
25. vitamin K.
26. vitamin E.

 

23. Marasmus is a form of protein-energy malnutrition characterized by
24. extreme wasting of muscles.
25. gain of abdominal adipose tissue.
26. severe edema in the extremities.
27. unusual growth of the jaw.

 

24. Kwashiorkor is a form of protein-energy malnutrition characterized by
25. extreme wasting of muscles.
26. gain of abdominal adipose tissue.
27. severe edema in the extremities.
28. unusual growth of the jaw.

 

25. The World Cancer Research Fund and the American Institute for Cancer Research recommend that people limit their intake of red meat to no more than 18 ounces every week and eat very little processed meat. These recommendations are explained by
26. the association of chronic high consumption of red meat or processed meats with increased risk of colorectal cancer.
27. the association of chronic high consumption of red meat or processed meats with increased risk of breast cancer.
28. the association of chronic high consumption of red meat or processed meats with increased risk of obesity, a risk factor for certain cancers.
29. the association of chronic high consumption of red meat or processed meats with increased risk of lung cancer.

 

 

 

Multiple Choice: Application Based

 

 

26. Animal-derived foods are considered to be more complete protein sources than plant-derived foods because
27. they contain all of the essential amino acids, while plant-derived foods contain no essential amino acids.
28. they contain all of the essential amino acids, while plant-derived foods contain low amounts of one or more of the essential amino acids.
29. they contain all 20 of the amino acids used for protein synthesis in the human body, while plant-derived foods contain only 11 amino acids.
30. they contain only essential amino acids, while plant-derived foods contain only nonessential amino acids.

 

27. The problem of a limiting amino acid is most simply overcome by
28. combining foods with different limiting amino acids to complement each other and provide adequate amounts of all the essential amino acids.
29. combining foods with the same limiting amino acid to increase the amount of that amino acid to an adequate level.
30. increasing portion size of a food with a limiting amino acid so that more of that amino acid is consumed.
31. reducing portion size of complete proteins so that the amount of the limiting amino acid is relatively increased.

 

28. An example of protein complementation is
29. steak and salmon.
30. rice and beans.
31. corn and rice.
32. whole grain and refined rice.

 

29. The shape of all proteins ranging from small, simple proteins to large, complex proteins is determined by
30. charge interactions.
31. moving outside the cell.
32. their amino acid sequences.
33. the addition of prosthetic groups.

 

30. A person’s _____ is found inside the cell. In contrast, a person’s _____ is what is outwardly apparent to another person.
31. genotype, phenotype
32. phenotype, genotype
33. DNA, protein profile
34. genetic mutation, genotype

 

31. A person’s _____ is largely determined by their _____.
32. phenotype, genotype
33. genotype, phenotype
34. height, phenotype

 

32. Alterations that change the sequence of information in a gene, leading to a change in the primary structure of a protein, are called
33. epigenetic modifications.
34. epigenetic changes.
35. transcriptional modifications.
36. mutations.

 

33. Alterations that modify a gene by changing its regulation but not the sequence of information are called
34. mutations.
35. phenotypic changes.
36. transcriptional modifications.
37. epigenetic modifications.

 

34. The phenomenon that explains why identical twins may differ in certain ways is most appropriately called
35. a mutation.
36. epigenetic variation.
37. sequential variation.
38. transcriptional variation.

 

35. Chemical digestion of protein begins in the stomach, where _____ denatures proteins and _____ begins to digest them into smaller pieces.
36. hydrochloric acid, pepsinogen
37. hydrochloric acid, pepsin
38. gastrin, hydrochloric acid
39. gastrin, pepsin

 

36. The complete digestion of proteins in the small intestine yields
37. only single amino acids that are absorbed across the absorptive cells into the blood.
38. single amino acids and di- and tripeptides that are broken down to single amino acids by protesases in the absorptive cells.
39. α-keto acids and amino groups that are reassembled in the absorptive cells prior to entering the blood.

 

37. Collagen is an example of
38. a structural protein.
39. a catalytic protein.
40. a hormone.
41. an immune protein.

 

38. In a protein-deficient state one cannot make _____ to fight off infectious agents.
39. albumin
40. hormones
41. enzymes
42. antibodies

 

39. When _____ production is reduced because of protein deficiency, _____ can result from fluid imbalance.
40. albumin, edema
41. protein, infection
42. collagen, arthritis
43. collagen, edema

 

40. Amino acids are not excreted intact. Rather,
41. the nitrogen-containing amino group is recycled while the remainder of the molecule is excreted in the urine.
42. the nitrogen-containing amino group is removed and converted to urea, which is excreted in the urine.
43. the carboxylic acid group is removed, neutralized by the bile, and excreted in the feces.
44. the side-chain group is removed and excreted while the reminder of the molecule is recycled.
45. Nitrogen balance studies are used to assess
46. protein status.
47. urea production.
48. protein absorption.
49. protein excretion.

 

42. During times of starvation or illness a nitrogen balance study would likely demonstrate
43. nitrogen balance.
44. negative nitrogen balance.
45. positive nitrogen balance.

 

43. During childhood or recovery from an illness, a nitrogen balance study would likely demonstrate
44. nitrogen balance.
45. negative nitrogen balance.
46. positive nitrogen balance.

 

44. The RDA for protein is 0.8 g/kg/day. Todd is 5’10” and weighs 80 kg (about 175 pounds). According to the RDA, he requires
45. 6.4 grams of protein per day.
46. 64 grams of protein per day.
47. 640 grams of protein per day.
48. none of the above; this cannot be determined based on the information provided.

 

45. The Acceptable Macronutrient Distribution Range (AMDR) for protein is 10 to 35% of total energy intake. If Hannah consumes 2,000 kcal/day, her range of protein intake should be
46. 5 to 18 g/day
47. 25 to 100 g/day
48. 50 to 175 g/day
49. 100 to 250 g/day

 

 

 

Answer Key                       Note: ANS = correct answer; REF = page reference; TOP = section/outcome

 

True/False

1. ANS: T REF: 101                       TOP: 5.1
2. ANS: T REF: 104                       TOP: 5.3
3. ANS: T REF: 107                       TOP: 5.3
4. ANS: F REF: 109                       TOP: 5.5
5. ANS: F REF: 110                       TOP: 5.5
6. ANS: T REF: 115                       TOP: 5.6
7. ANS: T REF: 115                       TOP: 5.6
8. ANS: T REF: 115                       TOP: 5.7
9. ANS: T REF: 117                       TOP: 5.8
10. ANS: T REF: 122                       TOP: 5.10

 

Multiple Choice

1. ANS: C REF: 99                         TOP: 5.1
2. ANS: A REF: 100                       TOP: 5.1
3. ANS: B REF: 100                       TOP: 5.1
4. ANS: A REF: 100                       TOP: 5.1
5. ANS: A REF: 102                       TOP: 5.1
6. ANS: C REF: 102                       TOP: 5.2
7. ANS: A REF: 103                       TOP: 5.2
8. ANS: B REF: 103                       TOP: 5.2
9. ANS: B REF: 104                       TOP: 5.2
10. ANS: B REF: 104                       TOP: 5.3
11. ANS: A REF: 107                       TOP: 5.3
12. ANS: B REF: 109                       TOP: 5.5
13. ANS: A REF: 110                       TOP: 5.5
14. ANS: B REF: 110                       TOP: 5.5
15. ANS: C REF: 110                       TOP: 5.5
16. ANS: A REF: 110                       TOP: 5.5
17. ANS: A REF: 110-111              TOP: 5.5
18. ANS: B REF: 113                       TOP: 5.6
19. ANS: A REF: 115                       TOP: 5.7
20. ANS: B REF: 116                       TOP: 5.7
21. ANS: C REF: 116                       TOP: 5.7
22. ANS: A REF: 119                       TOP: 5.9
23. ANS: A REF: 121                       TOP: 5.10
24. ANS: C REF: 121                       TOP: 5.10
25. ANS: A REF: 122                       TOP: 5.10
26. ANS: B REF: 102                       TOP: 5.1
27. ANS: A REF: 102                       TOP: 5.1
28. ANS: B REF: 102                       TOP: 5.1
29. ANS: C REF: 104-105              TOP: 5.3
30. ANS: A REF: 107-108              TOP: 5.4
31. ANS: A REF: 107-108              TOP: 5.4
32. ANS: D REF: 108                       TOP: 5.4
33. ANS: D REF: 108                       TOP: 5.4
34. ANS: B REF: 108                       TOP: 5.4
35. ANS: B REF: 109-110              TOP: 5.5
36. ANS: B REF: 110                       TOP: 5.5
37. ANS: A REF: 111                       TOP: 5.6
38. ANS: D REF: 113                       TOP: 5.6
39. ANS: A REF: 113                       TOP: 5.6
40. ANS: B REF: 115                       TOP: 5.7
41. ANS: A REF: 115-116              TOP: 5.7
42. ANS: B REF: 116                       TOP: 5.7
43. ANS: C REF: 116                       TOP: 5.7
44. ANS: B REF: 117                       TOP: 5.8
45. ANS: C REF: 117                       TOP: 5.8