Chapter 6-1

Understanding Nutrition 14th Edition

Whitney Solutions Manual
Full download at link:

Solution Manual: https://testbankpack.com/

Test Bank: https://testbankpack.com/

Chapter 6 – Protein: Amino Acids

Learning Objectives
After completing Chapter 6, the student will be able to:
6.1 Recognize the chemical structures of amino acids and proteins.
a. Describe how the chemical structure of proteins differs from the structures of carbohydrates and fats.
b. List the 9 essential amino acids.
6.2 Summarize protein digestion and absorption.
a. Trace the digestion of protein and list the enzymes needed to complete the process.
6.3 Describe how the body makes proteins and uses them to perform various roles.
a. Explain the process used by the body to synthesize new proteins.
b. List the major functions of protein in the body.
c. Describe nitrogen balance and provide examples of positive nitrogen balance, negative nitrogen
balance, and equilibrium.
d. Describe deamination, where it occurs in the body, the products produced, and the fate of these
products.
6.4 Explain the differences between high-quality and low-quality proteins, including notable food sources of
each.
a. Discuss the factors used to evaluate protein quality.
6.5 Identify the health benefits of, and recommendations for, protein.
a. Describe the problems that result from inadequate intake of protein and protein-kcalories.
b. Discuss the health effects of over-consumption of protein.
c. Calculate the protein needed daily using the RDA for protein.
d. Discuss the health risks of protein and amino acid supplements.
H6 Explain how nutrients influence gene activity (nutrigenomics) and how genes influence the activities of
nutrients (nutrigenetics).
a. Define nutritional genomics and explain its potential uses in health care.

Assignments and Other Instructional Materials

The following ready-to-use assignments are available in this chapter of the instructor’s manual:
• New! Case Study 6-1: Protein Adequacy
• Updated! Case Study 6-2: Amino Acid Supplements
• Worksheet 6-1: Significance of Amino Acids1
• Worksheet 6-2: Nitrogen Balance Calculations
• Worksheet 6-3: Quick Protein Intake Assessment2

1 Worksheets 6-1, 6-2, and 6-5 contributed by Daryle Wane

2 Worksheet 6-3 and Handouts 6-2 and 6-3 contributed by Sharon Rady Rolfes

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license distributed with a certain product or service or otherwise on a password-protected website for classroom use.
Chapter 6-2

• Worksheet 6-4: Chapter 6 Crossword Puzzle3

• Updated! Worksheet 6-5: Proteins from Foods (Internet Exercise)
• Critical thinking questions with answers
• New! Key Terms and Definitions
Other instructional materials in this chapter of the instructor’s manual include:
• Answer key for How To activity and study card questions
• Classroom activities, featuring a New! meal comparison activity (6-3)
• Worksheet answer keys (as appropriate)
Visit the book’s instructor companion website to download:
• Handout 6-1: Plant Proteins in Human Nutrition—Myths and Realities
• Handout 6-2: How to Use the Exchange System to Estimate Protein
• Handout 6-3: An Example of Enzyme Action

Glossary
Chapter Key Terms
➢ acidosis (assi-DOE-sis): higher-than-normal acidity in the blood and body fluids.
➢ acids: compounds that release hydrogen ions in a solution.
➢ alkalosis (alka-LOE-sis): higher-than-normal alkalinity (base) in the blood and body fluids.
➢ amino (a-MEEN-oh) acids: building blocks of proteins. Each contains an amino group, an acid group, a
hydrogen atom, and a distinctive side group, all attached to a central carbon atom.
o amino = containing nitrogen
➢ amino acid pool: the supply of amino acids derived from either food proteins or body proteins that collect
in the cells and circulating blood and stand ready to be incorporated in proteins and other compounds or
used for energy.
➢ ammonia: a compound with the chemical formula NH3; produced during the deamination of amino acids.
➢ antibodies: large proteins of the blood and body fluids, produced by the immune system in response to the
invasion of the body by foreign molecules (usually proteins called antigens). Antibodies combine with and
inactivate the foreign invaders, thus protecting the body.
➢ antigens: substances that elicit the formation of antibodies or an inflammation reaction from the immune
system. A bacterium, a virus, a toxin, and a protein in food that causes allergy are all examples of antigens.
➢ bases: compounds that accept hydrogen ions in a solution.
➢ branched-chain amino acids: the essential amino acids leucine, isoleucine, and valine, which are present
in large amounts in skeletal muscle tissue; falsely promoted as fuel for exercising muscles.
➢ buffers: compounds that keep a solution’s pH constant when acids or bases are added.
➢ collagen (KOL-ah-jen): the structural protein from which connective tissues such as scars, tendons,
ligaments, and the foundations of bones and teeth are made.
➢ complementary proteins: two or more dietary proteins whose amino acid assortments complement each
other in such a way that the essential amino acids missing from one are supplied by the other.
➢ deamination (dee-AM-ih-NAY-shun): removal of the amino (NH2) group from a compound such as an
amino acid.
➢ denaturation (dee-NAY-chur-AY-shun): the change in a protein’s shape and consequent loss of its
function brought about by heat, agitation, acid, base, alcohol, heavy metals, or other agents.
➢ dipeptide (dye-PEP-tide): two amino acids bonded together.
o di = two
o peptide = amino acid
➢ edema (eh-DEEM-uh): the swelling of body tissue caused by excessive amounts of fluid in the interstitial
spaces; seen in protein deficiency (among other conditions).
➢ enzymes: proteins that facilitate chemical reactions without being changed in the process; protein catalysts.
➢ essential amino acids: amino acids that the body cannot synthesize in amounts sufficient to meet
physiological needs. conditionally essential amino acid: an amino acid that is normally nonessential, but

3 Contributed by Carrie King.

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 Chapter 6-3

must be supplied by the diet in special circumstances when the need for it exceeds the body’s ability to
produce it.
➢ fluid balance: maintenance of the proper types and amounts of fluid in each compartment of the body
fluids (see also Chapter 12).
➢ gene expression: the process by which a cell converts the genetic code into RNA and protein.
➢ hemoglobin (HE-moh-GLO-bin): the globular protein of the red blood cells that transports oxygen from
the lungs to tissues throughout the body; hemoglobin accounts for 80 percent of the body’s iron.
o hemo = blood
o globin = globular protein
➢ high-quality proteins: dietary proteins containing all the essential amino acids in relatively the same
amounts that human beings require. They may also contain nonessential amino acids.
➢ immunity: the body’s ability to defend itself against diseases (see also Chapter 18).
➢ keto (KEY-toe) acid: an organic acid that contains a carbonyl group (C5O).

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Chapter 6-4

➢ limiting amino acid: the essential amino acid found in the shortest supply relative to the amounts needed
for protein synthesis in the body. Four amino acids are most likely to be limiting:
o Lysine
o Methionine
o Threonine
o Tryptophan
➢ matrix (MAY-tricks): the basic substance that gives form to a developing structure; in the body, the
formative cells from which teeth and bones grow.
➢ neurotransmitters: chemicals that are released at the end of a nerve cell when a nerve impulse arrives
there. They diffuse across the gap to the next cell and alter the membrane of that second cell to either
inhibit or excite it.
➢ nitrogen balance: the amount of nitrogen consumed (N in) as compared with the amount of nitrogen
excreted (N out) in a given period of time.
➢ nonessential amino acids: amino acids that the body can synthesize.
➢ pepsin: a gastric enzyme that hydrolyzes protein. Pepsin is secreted in an inactive form, pepsinogen, which
is activated by hydrochloric acid in the stomach.
➢ peptidase: a digestive enzyme that hydrolyzes peptide bonds. Tripeptidases cleave tripeptides;
dipeptidases cleave dipeptides. Endopeptidases cleave peptide bonds within the chain to create smaller
fragments, whereas exopeptidases cleave bonds at the ends to release free amino acids.
o tri = three
o di = two
o endo = within
o exo = outside
➢ peptide bond: a bond that connects the acid end of one amino acid with the amino end of another, forming
a link in a protein chain.
➢ polypeptide: many (10 or more) amino acids bonded together.
o poly = many
➢ proteases (PRO-tee-aces): enzymes that hydrolyze protein.
➢ protein digestibility: a measure of the amount of amino acids absorbed from a given protein intake.
➢ protein turnover: the degradation and synthesis of protein.
➢ proteins: compounds composed of carbon, hydrogen, oxygen, and nitrogen atoms, arranged into amino
acids linked in a chain. Some amino acids also contain sulfur atoms.
➢ reference protein: a standard against which to measure the quality of other proteins.
➢ serotonin (SER-oh-TONE-in): a neurotransmitter important in sleep regulation, appetite control, and
sensory perception, among other roles. Serotonin is synthesized in the body from the amino acid tryptophan
with the help of vitamin B6.
➢ sickle-cell anemia: a hereditary form of anemia characterized by abnormal sickle- or crescent-shaped red
blood cells. Sickled cells interfere with oxygen transport and blood flow. Symptoms are precipitated by
dehydration and insufficient oxygen (as may occur at high altitudes) and include hemolytic anemia (red
blood cells burst), fever, and severe pain in the joints and abdomen
➢ transamination (TRANS-am-ih-NAY-shun): the transfer of an amino group from one amino acid to a keto
acid, producing a new nonessential amino acid and a new keto acid.
➢ transcription: the process of messenger RNA being made from a template of DNA.
➢ translation: the process of messenger RNA directing the sequence of amino acids and synthesis of
proteins.
➢ tripeptide: three amino acids bonded together.
o tri = three
➢ urea (you-REE-uh): the principal nitrogen-excretion product of protein metabolism. Two ammonia
fragments are combined with carbon dioxide to form urea.
➢ whey protein: a by-product of cheese production; falsely promoted as increasing muscle mass. Whey is the
watery part of milk that separates from the curds.
Nutritional Genomics Terms
➢ chromosomes: structures within the nucleus of a cell made of DNA and associated proteins. Human beings
have46 chromosomes in 23 pairs. Each chromosome has many genes.
➢ DNA (deoxyribonucleic acid): the double helix molecules of which genes are made.

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 Chapter 6-5

➢ epigenetics: the study of heritable changes in gene function that occur without a change in the DNA
sequence.
➢ gene expression: the process by which a cell converts the genetic code into RNA and protein.
➢ genes: sections of chromosomes that contain the instructions needed to make one or more proteins.
➢ genetics: the study of genes and inheritance.
➢ genomics: the study of all the genes in an organism and their interactions with environmental factors.
➢ human genome (GEE-nome): the complete set of genetic material (DNA) in a human being.
➢ methylation: the addition of a methyl group (CH3).
➢ microarray technology: research tools that analyze the expression of thousands of genes simultaneously
and search for particular gene changes associated with a disease. DNA microarrays are also called DNA
chips.
➢ mutations: permanent changes in the DNA that can be inherited.
➢ nucleotide bases: the nitrogen containing building blocks of DNA and RNA—cytosine (C), thymine (T),
uracil (U), guanine (G), and adenine (A). In DNA, the base pairs are A–T and C–G and in RNA, the base
pairs are A–U and C–G.
➢ nucleotides: the subunits of DNA and RNA molecules, composed of a phosphate group, a 5-carbon sugar
(deoxyribose for DNA and ribose for RNA), and a nitrogen-containing base.
➢ nutritional genomics: the science of how nutrients affect the activities of genes (nutrigenomics) and how
genes affect the activities of nutrients (nutrigenetics).
➢ phenylketonuria (FEN-il-KEY-toe- NEW-ree-ah) or PKU: an inherited disorder characterized by failure
to metabolize the amino acid phenylalanine to tyrosine.
➢ proteome: all proteins in a cell. The study of all proteins produced by a species is called proteomics.
➢ RNA (ribonucleic acid): a compound similar to DNA, but RNA is a single strand with a ribose sugar
instead of a deoxyribose sugar and uracil instead of thymine as one of its bases.

Lecture Presentation Outline

Key to instructor resource annotations (shown to the right of or below outline topics):
Website = Available for download from book companion website: HN = student handout
IM = Included in this instructor’s manual: CS = case study, WS = worksheet, CA = classroom activity

Introductory/whole chapter resources: PL figure JPEGs; Test Bank; IM WS 6-4

I. The Chemist’s View of Proteins

A. Amino Acids – Explain amino acids, including: IM WS 6-1
1. Unique Side Groups (Figure 6-1 and 6-2)
2. Nonessential Amino Acids
3. Essential Amino Acids
4. Conditionally Essential Amino Acids
B. Proteins – Explain proteins, including:
1. Amino Acid Chains
a. Dipeptides (Figure 6-3)
b. Tripeptides
c. Polypeptides (Figure 6-4)
2. Primary Structure—Amino Acid Sequence – The sequence of amino acids varies greatly.
3. Secondary Structure—Polypeptide Shapes
a. Describe polypeptide structures
b. Explain the role of electrical attraction
4. Tertiary Structure—Polypeptide Tangles
a. Describe tertiary structures
b. Explain hydrophilic versus hydrophobic
5. Quaternary Structure—Multiple Polypeptide Interactions – Describe quaternary structures such as
hemoglobin (Figure 6-5)

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Chapter 6-6

6. Protein Denaturation – Explain protein denaturation

a. Proteins can be denatured by heat and/or acid
b. After a certain point, cannot be reversed
II. Digestion and Absorption of Proteins
A. Protein Digestion – Explain the digestion of protein in the following anatomical areas (Figure 6-6):
1. In the Stomach
a. Protein is denatured by hydrochloric acid
b. Pepsinogen
c. Pepsin
2. In the Small Intestine
a. Proteases
b. Peptidases
B. Protein Absorption
1. Used by intestinal cells for energy or synthesis of necessary compounds
2. Transported to the liver
3. Taking enzyme supplements or consuming predigested proteins is unnecessary
III. Proteins in the Body
A. Protein Synthesis – Explain the process of protein synthesis (Figure 6-7)
1. Synthesis is unique for each human being
2. Delivering the Instructions
a. Transcription
b. Translation
3. Lining Up the Amino Acids – Transfer RNA lines up the amino acids
4. Sequencing Errors – Can cause altered proteins (e.g., sickle-cell anemia; Figure 6-8)
5. Gene Expression
a. Cells regulate gene expression to make the type of protein needed for that cell
b. Diet influences gene expression
B. Roles of Proteins – Discuss the roles of proteins, including:
1. As Structural Materials
a. Matrix
b. Collagen
c. Cell replacement
2. As Enzymes (Figure 6-9) Website HN 6-3, CA 6-1
3. As Hormones (e.g., insulin)
4. As Regulators of Fluid Balance
a. Within cells and blood plasma
b. Edema
5. As Acid-Base Regulators
a. Acids
b. Bases
c. Buffers
d. Acidosis
e. Alkalosis
6. As Transporters IM CA 6-2
a. Carry lipids, vitamins, minerals, and oxygen in the body
b. Act as pumps in cell membranes (Figure 6-10)
7. As Antibodies
a. Fight antigens
b. Provide immunity
8. As a Source of Energy and Glucose – If needed
9. Other Roles
a. Blood clotting (fibrin)
b. Vision (opsin)

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 Chapter 6-7

C. A Preview of Protein Metabolism

1. Protein Turnover and the Amino Acid Pool
a. Protein turnover
b. Amino acid pool
2. Nitrogen Balance IM WS 6-2
a. Zero nitrogen balance
b. Positive nitrogen balance.
c. Negative nitrogen balance
3. Using Amino Acids to Make Other Compounds
a. Neurotransmitters
b. Tyrosine
c. Tryptophan
4. Using Amino Acids for Energy and Glucose
a. No readily available storage form of protein
b. Body breaks down tissue protein for energy
5. Using Amino Acids to Make Fat
a. Excess protein is deaminated and converted into fat
b. Nitrogen is excreted
6. Deaminating Amino Acids (Figure 6-11)
a. Nitrogen-containing amino groups are removed
b. Ammonia and keto acids
7. Using Amino Acids to Make Proteins or Nonessential Amino Acids
a. Cells can assemble amino acids into the protein needed
b. Transamination (Figure 6-12)
8. Converting Ammonia to Urea – Ammonia and carbon dioxide are combined in the liver to make urea
(Figure 6-13)
9. Excreting Urea (Figure 6-14)
a. Ammonia is converted to urea in the liver
b. The kidneys filter urea
c. Increased water intake is necessary with a high-protein diet
IV. Protein in Foods
A. Protein Quality
1. Digestibility – Depends on protein’s food source
a. Animal proteins 90%-99% absorbed
b. Plant proteins 70%-90% absorbed
c. Soy and legumes 90% absorbed
2. Amino Acid Composition
a. The liver can produce nonessential amino acids
b. Limiting amino acids
3. Reference Protein – The standard by which other proteins are measured
4. High-Quality Proteins
a. Contain all the essential amino acids
b. Animal foods contain all the essential amino acids
c. Plant foods tend to be missing one or more essential amino acids
B. Complementary Proteins IM HN 6-1
1. Combining plant foods that together contain all the essential amino acids
2. Used by vegetarians
V. Health Effects and Recommended Intakes of Protein IM CS 6-1, WS 6-5
A. Health Effects of Protein
1. Protein Deficiency
a. Lack of essential amino acids
b. Explain the health implications of a lack of protein

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Chapter 6-8

2. Heart Disease
a. Foods high in animal protein also tend to be high in saturated fat
b. Homocysteine levels increase cardiac risks
c. Arginine may protect against cardiac risks
3. Cancer – A high intake of animal protein is associated with some cancers
4. Adult Bone Loss (Osteoporosis)
a. High protein intake associated with increased calcium excretion
b. Inadequate protein intake affects bone health also
c. Ratio of calcium intake to protein intake may determine whether Ca loss is significant
5. Weight Control
a. High-protein foods are often high-fat foods
b. Protein at each meal provides satiety
c. Adequate protein, moderate fat, and sufficient carbohydrate better support weight loss
6. Kidney Disease
a. High protein intake increases the work of the kidneys
b. Does not seem to cause kidney disease
B. Recommended Intakes of Protein IM WS 6-3; Website HN 6-2
1. 10-35% energy intake
2. Protein RDA - 0.8 g/kg/day for most adults
3. Adequate Energy
a. Must consider energy intake
b. Must consider total grams of protein
C. From Guidelines to Groceries IM CA 6-3
1. Protein Foods
a. One ounce of protein food equals 7 grams of protein
b. 20% seafood
c. 70% meat, poultry, and eggs
d. 10% nuts, seeds, and legumes
2. Milk and Milk Products – 1 cup = ~8 g
3. Fruits, Vegetables, and Grains – Small amounts in vegetables and grains
D. Read Food Labels
1. Explain how to read the protein content on a food label
2. %DV represents quantity and quality
E. Protein and Amino Acid Supplements IM CS 6-2, CA 6-4
1. Many reasons for supplements
2. Protein Powders – Protein powders have not been found to improve athletic performance
a. Whey protein
3. Amino Acid Supplements – Amino acid supplements have no proven benefits for healthy people and
may be harmful
a. Branched-chain amino acids
b. Lysine
c. Tryptophan
VI. Highlight: Nutritional Genomics (Figure H6-1)
A. A Genomics Primer – Define and explain:
1. DNA (Figure H6-2)
2. Chromosomes
3. Nucleotide bases
4. RNA
5. Nucleotide
6. Gene expression (Figure H6-3)
7. Microarray technology
8. Epigenetics – Nutrients are involved in activating or suppressing genes without altering the gene itself

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 Chapter 6-9

B. Genetic Variation and Disease

1. Small differences in individual genomes
2. May affect the results of dietary modifications intended to manage/treat a disease
3. Personalization of recommendations
4. Single-Gene Disorders
a. Mutations cause alterations in single genes
b. Phenylketonuria
5. Multigene Disorders
a. Multiple genes are responsible for the disease
b. Heart disease
c. Genomic research
d. Single nucleotide polymorphisms (SNPs)
C. Clinical Concerns
1. An increased understanding of the human genome may impact health care by:
a. Increasing knowledge of individual disease risks
b. Individualizing treatment
c. Individualizing medications
d. Increasing knowledge of nongenetic causes of disease
2. Some question the benefit of identifying individual genetic markers
3. Even if specific recommendation can be made based on genes, some may choose not to follow
recommendations

Case Studies
Case Study 6-1: Protein Adequacy
Erin is a 28-year-old professional woman who is 5 feet 8 inches tall and vigilantly maintains her weight at 118
pounds by following a lacto-ovo (non-fat milk and egg whites only) vegetarian diet that supplies approximately
1200 calories a day. With her understanding that protein should provide between 10 and 35 percent of her daily
calories, she reasons that her daily intake of 40 grams of protein from milk, eggs, legumes, and nuts is adequate for
her needs. She is concerned, however, that she has been sick more than usual and has experienced two stress
fractures in her leg over the past three years while exercising.

1. What is the protein RDA per kilogram of healthy body weight?

a. 0.4 g
b. 0.6 g
c. 0.8 g
d. 1 g
e. 1.2 g

2. Assuming a healthy weight for Erin is 141 pounds, what is her recommended daily protein requirement?
a. 41 g
b. 46 g
c. 51 g
d. 56 g
e. 61 g

3. Remembering that protein provides 4 kcalories per gram, what percentage of Erin’s current total energy intake
comes from protein?
a. 7.3%
b. 9.3%
c. 11.3%
d. 13.3%
e. 15.3%

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Chapter 6-10

4. What percentage of total energy intake should come from protein?

a. 5 to 10%
b. 10 to 35%
c. 35 to 50%
d. 50 to 60%
e. 60 to 75%

5. What can be said about Erin’s protein intake?

a. Given that she is a lacto-ovo vegetarian, it is virtually impossible for her to get adequate, balanced protein.
b. She is actually getting more protein than recommended, and this may cause her to excrete calcium,
increasing her risk of bone fracture.
c. Erin’s reliance on legumes and other non-meat sources of protein may increase her risk of certain cancers,
such as colon cancer.
d. Although it falls within the recommended range in terms of the percentage of total energy intake, it is less
than recommended in terms of the absolute amount.
e. Given her lacto-ovo vegetarian diet, she is probably consuming too much methionine and tryptophan.

6. On average, an ounce of a protein food delivers how many grams of protein?

a. 1
b. 3
c. 5
d. 7
e. 9

7. Erin loves whole grains. Suppose she makes herself a snack from one serving of grains and one cup yogurt
topped with a serving of fresh strawberries. How much protein is in her snack?
a. 4 to 5 grams
b. 6 to 7 grams
c. 8 to 9 grams
d. 10 to 11 grams
e. 12 to 13 grams

Answer Key
1. c
2. c
3. d
4. b
5. d
6. d
7. d

Case 6-2: Amino Acid Supplements4

Danielle F. is a 78-year-old retired school teacher who is seeking ways to increase her protein intake. She does very
little cooking and avoids fish, poultry, and meat for personal reasons. She eats eggs occasionally but relies more on a
liquid amino acid product that claims to contain essential and non-essential amino acids in “naturally-occurring
amounts.”
Danielle decides to compare the protein quantity and quality of this product to an egg. Initially she learns that 1
whole egg contains 18 amino acids (9 essential amino acids and 9 non-essential amino acids). ½ teaspoon of liquid

4 Contributed by Barbara Quinn.

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 Chapter 6-11

amino acid product contains 16 amino acids (9 essential amino acids and 7 non-essential amino acids). Then she
examines the Nutrition Facts label for these two products. (See below.)

Egg Nutrition Facts Amino Acid Supplement Nutrition Facts

Nutrition Facts Nutrition Facts

Serving Size 1 egg (50g) Serving Size 1/2 tsp (2.5mL)
Servings Per Container 12
Amount Per Serving Amount Per Serving
Calories 70 Calories from Fat 45 Calories 0 Calories from Fat 0
% Daily Value* % Daily Value*
Total Fat 5g 8% Total Fat 0g 0%
Saturated Fat 1.5g 8% Trans Fat 0g
Polyunsaturated Fat 1g Cholesterol 0mg 0%
Monounsaturated Fat 2g Sodium 160mg 6%
Trans Fat 0g Total Carbohydrate 100mg 0%
Cholesterol 185mg 60% Protein 310mg
Sodium 70mg 3%
Vitamin A 0% • Vitamin C 0%
Potassium 70mg 2%
Calcium 0% • Iron 0%
Total Carbohydrate 0g 0%
Protein 6g 13%
Vitamin A 6% • Vitamin C 0%
Calcium 2% • Iron 4%
Vitamin D 10% • Thiamin 0%
Riboflavin 10% • Vitamin B6 4%
Folate 6% • Vitamin B12 8%
Phosphorus 10% • Zinc 4%

1. Danielle notices that protein is measured differently on the two Nutrition Facts labels. Knowing that 1 gram =
1000 milligrams, what can Danielle learn about the protein quantity of one serving of liquid amino acid as
compared to one whole egg?
2. Approximately how many teaspoons of liquid amino acid would Danielle need to eat every day to receive the
amount of protein in one egg? (Notice that the nutrition information for this product is for a ½ teaspoon
serving.)
3. Looking at the Nutrition Facts label, what other important nutrients besides protein will Danielle find in an egg
that are not present in her amino acid supplement?
4. What is the sodium content of an egg compared to one serving of the liquid amino acid product?
5. According to information in this chapter, what is the safest way for Danielle to obtain the protein and amino
acids she needs? Why?
6. What precautions should Danielle take regarding the use of amino acid supplements?

Answer Key
1. ½ teaspoon liquid amino acid = 310 milligrams or 0.31 grams protein. 1 egg = 6 grams or 6000 milligrams
protein. The egg provides over 19 times the protein as the supplement.
2. Approximately 10 teaspoons. ½ teaspoon contains 0.31 grams protein × 2 = 0.62 grams protein in 1 teaspoon ×
10 = 6.2 grams protein in 10 teaspoons liquid protein.
3. Answers may include vitamin A, vitamin D, B vitamins, calcium, zinc, and phosphorous.
4. 70 mg for 1 egg versus 160 mg for ½ teaspoon liquid amino acid—the supplement provides over twice the
sodium in a much smaller volume.

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Chapter 6-12

5. From food. Fat and carbohydrates in food facilitate the use of protein and amino acids in the body.
6. She should not exceed levels normally found in foods; large doses cause diarrhea; the body is not designed to
handle high concentrations or unusual combinations of amino acids.

Suggested Classroom Activities

Newcomers to nutrition too often think that improving nutritional status is simply a matter of introducing more
nutrients into the body. Some people think it is like dropping pennies into a jar—the more you put in, the more will
be there. They need to appreciate the enormous compensating ability of the body before they can understand how
little (or how much) nutrients affect nutritional status.

Classroom Activity 6-1: Illustration of Enzymatic Action5

Key concept: Action of enzymes Class size: Any
Instructions: Compare a chemical reaction in the body to the union of a bride and a groom. The union requires a
catalyst such as a priest or justice of the peace (JOP). The JOP has the power to unite the bride and groom and
performs the ceremony, but afterwards, goes on unchanged.

Classroom Activity 6-2: Demonstration of Diffusion and Active Transport 6

Key concept: Transfer of molecules across a membrane Class size: Any
Materials needed: Balloons (quantity = ½ the number of students)
Instructions: Divide the class physically in half with a space down the center (the cellular membrane). Demonstrate
diffusion by giving half the class small balloons to bounce up in the air (an area of higher concentration). A line of
students can then be placed in the “membrane” space to demonstrate how active transport assists in the process of
transferring the “molecule” balloons.

Classroom Activity 6-3: Protein Options (Meal Comparison)7

Key concept: Applying protein recommendations to food choices Class size: Any
Instructions: Present the three dinner meal plans below to students and use the discussion questions to prompt them
to evaluate the plans.
Dinner #1 Dinner #2 Dinner #3
Pot roast, beef, 3 oz Frittata with spinach, potatoes & Chipotle bean burrito (~2/3 cup
Mashed potatoes, ½ cup leeks, 1/6 of 10” pie black beans, 2.6 oz cheese,
Corn, ½ cup Corn, ½ cup lettuce, tomato)
Dinner roll, whole-wheat, 1 item Dinner roll, whole-wheat, 1 item Corn, ½ cup
Kiwi, sliced, ½ cup Kiwi, sliced, ½ cup Kiwi, sliced, ½ cup
1% milk, 1 cup 1% milk, 1 cup 1% milk, 1 cup

Discussion questions:
1. Calculate the protein needs for a 25-year-old female who weighs 110 pounds using the RDA of 0.8 g/kg. Which
of the dinner meal plans would provide at least 50% of her daily need for protein? How does this illustrate how
easy it is to consume excess protein?
2. Which of the meal plans is primarily high-quality protein? Low-quality protein?
3. How can you modify the meal plans for vegetarians so that they fit the vegetarian meal plans reviewed in
Chapter 1?
4. Does the protein content of any of the foods surprise you?
Answer key:
1. 0.8 g/kg × 50 kg = 40 grams protein. Each meal provides greater than 50% of her daily need for protein. It is
relatively common to consume more protein than is needed.
2. Dinners #1 and #2 are high-quality protein (primarily animal-based), dinner #3 is lower-quality protein
(primarily plant-based).

5 Activity provided by: Robin S. Bagby, M. Ed., R.D., Penn State Nutrition Center
6 Activity provided by: Dorothy G. Herron, Orangeburg-Calhoun Technical College
7
Contributed by Carrie King

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 Chapter 6-13

3. Answers will vary. Possible examples: Dinner #3: replace the cow’s milk with soy milk and remove the cheese
from the burrito to make it a vegan meal; dinners #2 and #3 would be appropriate for lacto-ovo-vegetarian meal
plans.
4. Discuss the protein content of the various foods in the meal plan.
Nutrient composition of meals for instructor reference:
Dinner #1 Menu Item Cal Pro CB Fe
Pot roast, beef, 3 oz 262 24 0 2.4
Mashed potatoes, ½ cup 120 2 15 0.027
Corn, ½ cup 72 2.5 16 0.33
Dinner roll, whole-wheat, 1 item 74 2.4 14 0.68
Kiwi, sliced, ½ cup 55 1 13 0.28
1% milk, 1 cup 102 8 12 0.07
Totals 685 39.9 70 4.03

Dinner #2 Menu Item Cal Pro CB Fe

Frittata with spinach, potatoes & leeks, 1/6 of 10” pie 185 12.5 18.9 3.0
Corn, ½ cup 72 2.5 16 0.33
Dinner roll, whole-wheat, 1 item 74 2.4 14 0.68
Kiwi, sliced, ½ cup 55 1 13 0.28
1% milk, 1 cup 102 8 12 0.07
Totals 488 26.4 73.9 4.36

Dinner #3 Menu Item Cal Pro CB Fe

Chipotle bean burrito (~2/3 cup black beans, 2.6 oz cheese, 361 16.8 52.2 3.3
lettuce, tomato)
Corn, ½ cup 72 2.5 16 0.33
Kiwi, sliced, ½ cup 55 1 13 0.28
1% milk, 1 cup 102 8 12 0.07
Totals 590 28.3 93.2 3.98

Key: Cal = kcalories, Pro = protein (grams), CB = carbohydrate (grams), Fe = iron (milligrams)

Classroom Activity 6-4: Protein Content of Over-the-Counter Protein and Amino Acid Supplements
Key concepts: Protein sources; protein/amino acid supplements Class size: Any
Instructions: Protein powder supplements are marketed as providing substantial amounts of protein and enhancing
athletic performance. Instruct students to go to the grocery or drug store and record the following regarding the
protein powder supplements they locate: name of supplement, cost of supplement, recommended daily dose, protein
content of suggested dose, and the percent of the DV for protein per serving/dose. Discuss in class and generate
suggestions for more safe, effective, enjoyable, and economical choices through food intake.

How To “Try It” Activities Answer Key

How to Calculate Recommended Protein Intakes
The student should first determine the weight to use: her or his weight in kg if within the healthy BMI range, or if
not, then the weight at the midpoint of the healthy BMI range for a person of her/his height. The student should then
multiply her or his weight in kg by 0.8 g/kg (or 0.85 g/kg if only 17 or 18 years old) to determine the protein RDA.
For example, a 19-year-old student who is 5’6” and weighs 115 lb. (BMI = 18.6) would use his/her current weight
and calculate an RDA of 42 g protein per day.

Study Card 6 Answer Key

1. The primary structure of a protein is determined by the sequence of amino acids. The secondary structure of
proteins is determined by weak electrical attractions within the polypeptide chain. As positively charged
hydrogens attract nearby negatively charged oxygens, sections of the polypeptide chain twist into a helix or fold

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Chapter 6-14

into a pleated sheet, for example. The tertiary structure of proteins occurs as long polypeptide chains twist and
fold into a variety of complex, tangled shapes. The unique side group of each amino acid gives it characteristics
that attract it to, or repel it from, the surrounding fluids and other amino acids. Some amino acid side groups are
attracted to water molecules; they are hydrophilic. Other side groups are repelled by water; they are
hydrophobic. As amino acids are strung together to make a polypeptide, the chain folds so that its hydrophilic
side groups are on the outer surface near water; the hydrophobic groups tuck themselves inside, away from
water. Thus, the sequence of amino acids determines how the completed protein will fold and twist into its final
shape.
2. Essential amino acids are the nine amino acids that the human body either cannot make at all or cannot make in
sufficient quantity to meet its needs.
3. a 4. c 5. a
6. Enzymes are proteins that facilitate chemical reactions without being changed in the process (catalysts). As
facilitators, enzymes help to break down substances, build substances (such as bone), and transform one
substance into another (amino acids into glucose, for example). Whereas all enzymes are proteins, only some
hormones are. Hormones, chemical messengers, are not direct and unchanging facilitators of chemical
reactions; rather, they elicit the appropriate responses to restore and maintain normal conditions.
7. In the body, amino acids can be used to make body proteins or other nitrogen-containing compounds, or they
can be stripped of their nitrogen and used for energy (either immediately or stored as fat for later use).
Deamination is the removal of the amino (NH2) group from a compound such as an amino acid—the first step
in catabolizing an amino acid for energy or converting it to fat. Nitrogen balance is the amount of nitrogen
consumed (N in) as compared with the amount of nitrogen excreted (N out) in a given period of time. Zero
nitrogen balance is associated with being an adult in good health. Nitrogen status is positive in growing infants,
children, adolescents, pregnant women, and people recovering from protein deficiency or illness; their nitrogen
intake exceeds their nitrogen excretion. Nitrogen status is negative in people who are starving or suffering other
severe stresses such as burns, injuries, infections, and fever; their nitrogen excretion exceeds their nitrogen
intake.
8. a 9. c 10. c
11. In general, plant proteins are lower quality than animal proteins, and plants also offer less protein (per weight or
measure of food). For this reason, many vegetarians improve the quality of proteins in their diets by combining
plant-protein foods that have different but complementary amino acid patterns. This strategy yields
complementary proteins that together contain all the essential amino acids in quantities sufficient to support
health. Vegetarians can receive all the amino acids they need over the course of a day by eating a variety of
whole grains, legumes, seeds, nuts, and vegetables.
12. a
13. Selecting too many protein-rich foods may crowd out fruits, vegetables, and whole grains, making the diet
inadequate in other nutrients. A high-protein diet may contribute to the progression of heart disease. Foods rich
in animal protein also tend to be rich in saturated fats, and there is a correlation between animal-protein intake
(red meats and dairy products) and heart disease. On the other hand, substituting vegetable protein for animal
protein may improve blood pressure and blood lipids and decrease heart disease mortality. Research suggests
that elevated levels of the amino acid homocysteine may be an independent risk factor for heart disease, heart
attacks, and sudden death in patients with heart disease, but researchers do not yet fully understand the many
factors that can raise homocysteine in the blood or whether elevated levels are a cause or an effect of heart
disease. The amino acid arginine may help protect against heart disease by lowering blood pressure and
homocysteine levels. Evidence suggests a strong correlation between high intakes of red meat and processed
meats with cancer of the colon. When protein intake is high, calcium excretion increases, but whether excess
protein depletes bone calcium may depend upon the ratio of calcium intake to protein intake. Some (but not all)
research suggests that animal protein may be more detrimental to calcium metabolism and bone health than
vegetable protein. A high protein intake may also accelerate kidney deterioration in people with chronic kidney
disease.
14. In setting protein recommendations, the authorities consider the two reasons the body needs dietary protein:
First, dietary protein is the only source of the essential amino acids, and second, it is the only practical source of

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 Chapter 6-15

nitrogen with which to build the nonessential amino acids and other nitrogen-containing compounds the body
needs. The RDA covers the needs for replacing worn-out tissue, so it increases for larger people; it also covers
the needs for building new tissue during growth, so it increases for infants, children, adolescents, and pregnant
and lactating women. In setting the RDA, the DRI Committee assumes that people are healthy and do not have
unusual metabolic needs for protein, that the protein eaten will be of mixed quality (from both high- and low-
quality sources), and that the body will use the protein efficiently. In addition, the committee assumes that the
protein is consumed along with sufficient carbohydrate and fat to provide adequate energy and that other
nutrients in the diet are also adequate.
15. Branched-chain amino acid supplements may be beneficial for individuals with certain conditions such as liver
disease. Tryptophan may be effective for inducing drowsiness in insomniacs, but caution is still advised. For
other people, supplements do not offer benefits over consuming foods providing the equivalent amounts of
proteins or amino acids. Foods provide many other important nutrients with the protein. Large doses of amino
acids cause diarrhea. An excess of one amino acid can create such a demand for a carrier that it limits the
absorption of another amino acid, presenting the possibility of a deficiency. Amino acids that most successfully
attach to carriers enter in excess, creating the possibility of toxicity. Large doses of branched-chain amino acids
can raise plasma ammonia concentrations, which can be toxic to the brain.
16. b 17. d 18. a

Critical Thinking Questions8

1. What characteristics account for the complexity of proteins as a macronutrient as compared with carbohydrates
and lipids?
2. How would you explain to an individual the role of protein in the development of edema?
3. Compare the nitrogen balance state of a healthy adolescent female, aged 16, with that of a 45-year-old, healthy
male adult.
4. What is the significance of increased high-quality protein consumption in the American diet? Are there any
dietary strategies to enhance quality protein consumption other than direct consumption of high-quality
proteins?
5. The relationship between protein and health is complex. Functional protein deficiency states can lead to
significant disease processes, and yet there is also clinical evidence that certain proteins may be linked to the
development of chronic conditions such as cardiac disease. How can protein be considered to be both beneficial
and detrimental at the same time?
6. How would you provide adequate dietary protein for an individual diagnosed with renal disease?

Answer Key
1. Even though the body must break down all macronutrients into constituent parts to facilitate energy metabolism,
proteins are more complex in nature when compared to carbohydrates and lipids. In terms of chemical structure
and composition, proteins contain nitrogen, unlike carbohydrates and lipids. The side group attached to the
central carbon unit of each of the amino acids (the basic building blocks of proteins) is the major contributor to
a protein’s complexity. Each side group is considered to be unique. This is in contrast to complex
polysaccharide molecules such as starch in which each individual unit is the same glucose molecule. Even
though there is a different chemical group arrangement for lipids there are fewer lipid structures as compared to
protein structures. In addition, the sequencing of proteins consists of long amino acid chains based on individual
genetic profiles. The genetic information is delivered through a complex interaction of DNA and RNA
molecules. Errors in translation and transcription are possible and affect delivery of the genetic message.
2. The serum level of protein in the body plays a critical role in the regulation of water balance. If there are protein
deficiencies, fluid is more likely to shift from intravascular into interstitial spaces, resulting in a physiological
mechanism that leads to the cyclical presence of edema. This is because serum proteins such as albumin attract
water and help retain it within blood vessels. Deficiencies in protein can result in decreased colloid osmotic

8 Contributed by Daryle Wane.

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Chapter 6-16

pressure, leading to fluid shifting. Protein losses due to illness and/or disease processes similarly result in
edema. Additionally, if the liver is compromised through disease, then declined protein synthesis can lead to the
development of edema. Increased capillary permeability as a result of changes in oncotic pressure will lead to
protein leakage and edema development.
3. An adolescent female would be considered to be in a positive nitrogen balance state due to the fact that the
adolescent period is one of growth and development. Positive nitrogen balance favors the retention of nitrogen
(and protein) to promote growth functions. A 45-year-old male adult would be considered, if healthy, to be in
zero nitrogen balance (equilibrium).
4. The ingestion of high-quality proteins in the diet enables the body to effectively utilize all essential amino acids.
High-quality proteins are digested more easily as compared to low-quality proteins. High-quality proteins, by
virtue of containing essential amino acids, facilitate the numerous functions of proteins in the human body.
High-quality proteins are typically of animal content. A complementary protein strategy whereby a combination
of different foods eaten in the same day provides essential amino acids is an additional method that enhances
quality protein consumption. This method is utilized effectively in vegetarian diets to meet protein
requirements.
5. The genetic expression of protein is a basic requirement of life. Protein assumes various roles in the body that
are critical to life, such as: growth, structure, enzymes, hormones, fluid/electrolyte/acid-base balance, transport,
immune function (antigen/antibodies), and as an energy source. If there are differences in protein sequencing,
various abnormalities can occur. Protein deficiency states throughout the life cycle can result in various
alterations in growth and development patterns. Alterations in immune function can also occur, resulting in an
increase in infections. Inadequate protein levels can lead to altered ability of enzymes to function effectively in
the body. Deficiencies of protein can also affect pH regulation, resulting in altered biochemical reactions in the
body.
Consumption of protein in excess has also been demonstrated to place a burden on the heart when it comes from
animal sources that contain saturated fat. A specific protein that has been linked to heart disease is
homocysteine; however, though a correlation has been observed, it is unknown whether homocysteine is a cause
or an effect of heart disease. There is also an inverse relationship reported between increased homocysteine
levels and decreased B vitamins. Thus, there may be other factors that affect cardiac disposition rather than a
direct protein effect. Therefore, protein can be viewed as being beneficial in terms of supportive functions and
yet potentially detrimental if taken in excess, at least from certain foods.
6. Renal impairment can lead to altered ability to eliminate waste products of metabolism. As protein contains
nitrogen as a unique element, the consumption and breakdown of this nutrient can be affected by the kidney’s
inability to excrete urea. Buildup of nitrogenous end-products of metabolism can affect all body systems,
resulting in complex alterations of fluid and electrolyte balance. However, protein intake is essential to life and
well-being, and thus a protein intake of primarily high-quality proteins based on weight-based standards is
appropriate. Restriction and/or limitation of dietary protein may be prescribed because excess protein can
accelerate the decline in kidney function. Medical nutrition therapy facilitated by a dietician and health care
provider is necessary in order to manage and treat fluid and electrolyte imbalances.

IM Worksheet Answer Key

Worksheet 6-1: Significance of Amino Acids
Client Essential Non-essential Conditionally Sequencing Error
Required
Newborn baby X X X
diagnosed with ↑ Phenylalanine ↓ Tyrosine Autosomal
PKU recessive disorder
Elderly female X* X* X*
diagnosed with Variable amino Variable amino Variable amino
PEM acids levels seen → acids levels seen → acids levels seen →
usually decreased usually decreased usually decreased

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 Chapter 6-17

Client Essential Non-essential Conditionally Sequencing Error

Required
Adult male client X
with partial Branched-chain
thickness burns amino acids
over 20% BSA (leucine, valine &
isoleucine)
Glutamine
*Reference: http://ageing.oxfordjournals.org/cgi/reprint/26/6/457.pdf

Worksheet 6-2: Nitrogen Balance Calculations

1a. 135/2.2 = 61 kg; 61  0.8 g/kg = 49 g
1b. NI = 38/6.25 = 6.08; NL = 8 + 4 = 12; NB = 6.08 – 12 = -5.92
1c. Negative nitrogen balance.
1d. Recommended protein intake is 49 g/day, but client only took in 38 grams. Client took in too little protein, but
even with the recommended protein intake, the client would still be in negative nitrogen balance.
2a. 142/2.2 = 65 kg; 65  0.8 kg = 52 g
2b. NI = 69/6.25 =11.04; NL = 6 + 4 = 10; NB = 11.04 - 10 = 1.04
2c. Positive nitrogen balance.
2d. Recommended protein intake is 52 g/day, but client took in 69 grams. Client took in too much protein, but even
with the recommended protein intake, the client would still be in positive nitrogen balance.

Worksheet 6-3: Quick Protein Intake Assessment – Answers will vary.

Worksheet 6-4: Chapter 6 Crossword

1. nutrigenomics 4. calcium 7. antibodies 10. genetic information
2. small intestine 5. carbohydrates 8. high quality 11. urea
3. side group 6. amino acids 9. denaturation 12. nonessential

Worksheet 6-5: Proteins from Foods (Internet Exercise)

1. b 4. a 7. b
2. a 5. a
3. d 6. a

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Chapter 6-18

Worksheet 6-1: Significance of Amino Acids

Amino Acid Concept Application

Essential Must be provided to the body in that form; absence is incompatible with life
Non-essential Can be made by the body using other sources
Conditionally required In times of stress and/or growth and maturation events, non-essential amino acids
now become essential to the body
Sequencing errors Congenital disease such as sickle cell anemia is an example of a genetic disease
arising from alterations in genetic coding (amino acid substitution)

For each of the following clinical examples, indicate whether the client is at risk to develop a problem related to
amino acids.

Client Essential Non-Essential Conditionally Sequencing Error

Required
Newborn baby
diagnosed with
PKU

Elderly female
diagnosed with
PEM

Adult male client

with partial
thickness burns over
20% BSA

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 Chapter 6-19

Worksheet 6-2: Nitrogen Balance Calculations

Nitrogen Balance Studies

Nitrogen Balance (NB) = Nitrogen Intake (NI) – Nitrogen Loss (NL)

NB > -5 g/day = severe stress
NB = 0 to -5 g/day = moderate stress

NI = Protein intake (g/day ÷ 6.25)

NL = Urinary Urea Nitrogen (UUN, in g/day) + 4 g
UUN is derived from a 24-hour urine specimen
Normal range = 6-17 grams/24 hours

+ NB = anabolic state with a net gain in body protein

- NB = catabolic state with a net loss in body protein

For each of the following examples:

a. Calculate the client’s recommended protein intake.
b. Calculate the client’s NB.
c. Indicate whether the client is in + or – nitrogen balance.
d. Discuss the implications of the findings.

1. 45-year-old female, weight 135 lbs., protein intake of 38 grams and UUN = 8 grams

a.

b.

c.

d.

2. 89-year-old male, weight 142 lbs., protein intake of 69 grams and UUN = 6 grams

a.

b.

c.

d.

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Chapter 6-20

Worksheet 6-3: Quick Protein Intake Assessment

Most people in the United States and Canada receive more protein than they need. This is not
surprising considering the abundance of food eaten and the central role meats hold in the North
American diet. Using a 1-day food diary, estimate your protein intake for the day. Multiply the
number of servings you consumed by the estimated protein per serving to guesstimate your total
protein intake.

Food group Amount consumed Estimated protein Totals

Grains 3 grams/ounce

Vegetables 2 grams/cup equivalent

Fruit 0 grams/cup equivalent

Milk, yogurt, and 8 grams/cup equivalent

cheese
Meat, poultry, fish, dry 7 grams/ounce
beans, eggs and nuts
Oils, solid fats, and 0 grams/teaspoon
added sugars

Total estimated protein intake:

The protein RDA for young adults (19 to 24 years old) is 46 grams for women and 58 grams for
men. Health experts advise people to maintain moderate protein intakes—between the RDA and
twice the RDA.

1. Do you receive enough, but not too much, protein daily?

2. How often do you select plant-based protein foods?

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 Chapter 6-21

Worksheet 6-4: Chapter 6 Crossword Puzzle

1 2

3 4

5 6

8 9

10

11

12

Across: Down:
3. Distinguishing feature of the protein chemical 1. The study of how nutrients influence gene activity
structure 2. Body organ where the majority of proteins are
10. DNA contains the _____ that tells the body how to disassembled into amino acids
assemble proteins. 4. Increased dietary protein intake can lead to
11. When dietary protein intake increases the body’s increased excretion of the mineral _____.
production of _____ increases. 5. Amino acids can be used to make glucose if
12. Refers to amino acids that the body is able to insufficient dietary _____ are consumed.
manufacture 6. What the body uses to assemble its own proteins
7. Proteins that act to defend the body from disease
8. Proteins that provide sufficient quantities of
essential amino acids are referred to as _____.
9. What happens when proteins are exposed to heat
or acid such as stomach acid

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Chapter 6-22

Worksheet 6-5: Proteins from Foods (Internet Exercise)

Go to the following website to answers questions 1-3:
http://www.cdc.gov/nutrition/everyone/basics/protein.html. Do not close the window until you have
answered all of the questions.

On the website, click on Protein to answer questions 1 through 3.

1. Complementary proteins, when combined, do not include all of the essential amino acids.
a. True
b. False

2. Research studies have refuted the idea that foods must be eaten at the same meal to achieve the
concept of complementary proteins.
a. True
b. False

3. Approximately how many grams of protein does one cup of dry beans contain?
a. 4 grams of protein
b. 8 grams of protein
c. 11 grams of protein
d. 16 grams of protein
e. 21 grams of protein

Use the following website to answer questions 4-7: http://www.hsph.harvard.edu/nutritionsource/what-

should-you-eat/protein/.

4. For adults, the daily recommendation for protein is 0.8 grams per kilogram of body weight (g/kg).
a. True
b. False

5. The building blocks of protein are amino acids.

a. True
b. False

6. There is a link between red meat consumption and an increased risk of cardiovascular disease.
a. True
b. False

7. For men over 19 years of age, the recommended daily allowance (RDA) for protein is 80 grams.
a. True
b. False

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