Proteins and Amino Acids

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What Are Proteins?
 Large molecules
 Made up of chains of amino acids
 Are found in every cell in the body
 Are involved in most of the body’s functions and life
processes
 The sequence of amino acids is determined by DNA

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Structure of Proteins
 Made up of chains of amino acids; classified by number of
amino acids in a chain
• Peptides: fewer than 50 amino acids
- Dipeptides: 2 amino acids
- Tripeptides: 3 amino acids
- Polypeptides: more than 10 amino acids
• Proteins: more than 50 amino acids
- Typically 100 to 10,000 amino acids linked together
 Chains are synthesizes based on specific bodily DNA
 Amino acids are composed of carbon, hydrogen, oxygen,
and nitrogen

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Structural Differences Between Carbohydrates,
Lipids, and Proteins

Figure 6.1
The Anatomy of an Amino Acid

Figure 6.2b
Peptide Bonds Link Amino Acids
 Form when the acid group (COOH) of one amino acid joins
with the amine group (NH2) of a second amino acid
 Formed through condensation
 Broken through hydrolysis

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Condensation and Hydrolytic Reactions

Figure 6.3
Essential, Nonessential, and Conditional
 Essential – must be consumed in the diet
 Nonessential – can be synthesized in the body
 Conditionally essential – cannot be synthesized due to
illness or lack of necessary precursors
• Premature infants lack sufficient enzymes needed to
create arginine

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Structure of the Protein
 Four levels of structure
• Primary structure
• Secondary structure
• Tertiary structure
• Quaternary structure

Any alteration in the structure or sequencing changes

the shape and function of the protein

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Denaturing
 Alteration of the protein’s shape and thus functions through
the use of
• Heat
• Acids
• Bases
• Salts
• Mechanical agitation
 Primary structure is unchanged by denaturing

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Denaturing a Protein

Figure 6.5
Quick Review
 Proteins are chains of combination of amino acids
 Amino acids contain carbon, hydrogen, oxygen, nitrogen,
and sometimes sulfur
 Unique amino acids consist of a central carbon with a
carboxyl group, a hydrogen, a nitrogen-containing amine
group, and a unique side chain
 There are 20 side chains and 20 unique amino acids
• 9 essential amino acids
• 11 nonessential amino acids
- At time these become conditionally essential
 Amino acids link together with peptide bonds by
condensation and break apart by hydrolysis
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Quick Review
 Attractions and interactions between the side chains cause
the proteins to fold into precise three-dimensional shapes
 Protein shape determines its function
 Proteins are denatured and their shapes changed by
• Heat
• Acids
• Bases
• Salts
• Mechanical agitation

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Protein Digestion: Part 1

Figure 6.6
Protein Digestion: Part 2

Figure 6.6
Protein Digestion: Part 3

Figure 6.6
Protein Digestion: Part 4

Figure 6.6
Amino Acid Absorption
 Amino acids are absorbed in the small intestine
 Amino acids are transported to the liver from the intestines
via the portal vein
 In the liver, amino acids are
• Used to synthesize new proteins
• Converted to energy, glucose, or fat
• Released to the bloodstream and transported to cells
throughout the body
 Occasionally proteins are absorbed intact

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Amino Acid Metabolism
 Liver metabolizes amino acids, depending on bodily needs
 Most amino acids are sent into the blood to be picked up
and used by the cells
• Amino acid pool is limited but has many uses
 Protein turnover – the continual degradation and
synthesizing of protein

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Protein Synthesis

Figure 6.8
Deamination
 When the amino acid pool reaches capacity the amino acids
are broken down to their component parts for other uses
 First deamination must occur
 Carbon-containing remnants are
• Converted to glucose, if they are glucogenic amino acids,
through gluconeogensis
• Converted to fatty acids and stored as triglycerides in
adipose tissue

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Metabolic Fate of Amino Acids

Figure 6.7
Quick Review
 During digestion
• Proteins are broken down to amino acids with the help of
- Gastric juices
- Enzymes in the stomach and small intestine
- Enzymes from the pancreas and small intestine lining
 Limited supply of amino acids exist in the amino acid pool
 The amino acid pool acts as a reservoir for protein synthesis
 Surplus amino acids are
• Deaminated
- Used for glucose or energy
- Stored as fat
- Nitrogen is converted to urea and excreted in urine

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How Does the Body Use Protein?
 Functions of protein
• Provide structural and mechanical support
• Maintain body tissues
• Functions as enzymes and hormones
• Help maintain acid base balance
• Transport nutrients
• Assist the immune system
• Serve as a source of energy when necessary

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Quick Review
 Protein plays many important roles in the body, including:
• Helping facilitate muscular contraction
• Promoting satiety and appetite control

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How Much Protein Do You Need?
 Healthy, nonpregnant adults
• Should consume enough to replace what is used every
day
• The goal is nitrogen balance
 Pregnant woman, people recovering from surgery or injury,
and growing children
• Should consume enough to build new tissue

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Nitrogen Balance and Imbalance

Figure 6.12
Not All Protein Is Created Equal
 High quality protein
• Is digestible
• Contains all essential amino acids
• Provides sufficient protein to synthesize nonessential
amino acids
 It helps to be aware of:
• Amino acid score
• Limiting protein
• Protein digestibility corrected amino acid score
(PDCAAS)
• Biological value of protein rates absorption and retention
of protein for use
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Protein Quality
 Complete proteins
• Contain all nine essential amino acids
• Usually animal source are complete proteins
• Are considered higher quality
 Incomplete proteins
• Low in one or more essential amino acid
• Usually plant sources are incomplete

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Protein Needs
 Protein intake recommendations
• 10–35% of total daily kilocalories
• Adults over 18
- 0.8 g/kg daily

 American College of Sports Medicine, the American

Dietetic Association, and other experts advocate
• 50–100% more protein for competitive athletes
participating in endurance exercise or resistance exercise
• Typically this population eats more and therefore gets
additional protein

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Quick Review
 Protein quality is determined by digestibility and types and
amounts of amino acids
 Animal protein is more easily digested and complete
 Plant proteins are typically incomplete, except soy
 Plant proteins can be complemented with proteins from
other plant sources or animal source to improve their
quality
 Adults should consume 0.8 g/kg/d of protein
 Men and women in the United States tend to over consume
protein

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Best Sources of Protein
 Proteins are abundant in
• Dairy foods
• Meats
• Poultry
• Meat alternatives such as dried beans, peanut butter,
nuts, and soy
 3 oz serving of cooked meat, poultry, or fish
• Provides 21–25 grams of protein
• About 7 g/oz
• About the size of a deck of cards
• Adequate amount for one meal

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Best Sources of Protein

Figure 6.14
Quick Review
 A well-balanced diet can meet daily protein needs
 Best source of protein are animal products
• Eggs
• Lean meats
• Low-fat or fat-free dairy products
 Plant proteins such as soy, grains, and vegetables supply
substantial proteins
 Most people consume adequate protein from their diet and
do not need protein supplements

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Protein Bars
 Are marketed as convenient and portable
 Can be
• High in saturated fat and/or sugar
• Low in fiber
• Expensive
 A peanut butter sandwich is portable and lower in saturated
fat and sugar and higher in fiber than some protein bars

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Eating Too Much Protein
 Risk of heart disease
 Risk of kidney stones
 Risk of calcium loss from bones
 Risk of colon cancer
 Displacement of other nutrient-rich, disease preventing
foods

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Eating Too Little Protein
 Protein-energy malnutrition (PEM)
• Protein is used for energy rather than its other functions
in the body
• Other important nutrients are in short supply
• More prevalent in infants and children
- 17,000 children die each day as a result

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Too Little Protein
 Without adequate protein
• Cells lining the GI tract are not sufficiently replaced as
they slough off
• Digestive function is inhibited
• Absorption of food is reduced
• Intestinal bacteria gets into the blood and causes
septicemia
• Immune system is compromised due to malnutrition and
cannot fight infection

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Types of PEM: Kwashiorkor
 Severe protein deficiency
• Generally result of a diet high in
grains and deficient in protein
 Symptoms range from
• Edema in legs, feet, and stomach
• Muscle tone and strength
diminish
• Hair is brittle and easy to pull out
• Appear pale, sad, and apathetic
• Prone to infection, rapid heart
rate, excess fluid in lungs,
pneumonia, septicemia, and
water and electrolyte imbalances
(Image from http://www.thachers.org/pediatrics.htm)

Figure 6.16
Types of PEM: Marasmus
 Results from a severe deficiency
in kilocalories
• Frail, emaciated appearance
• Weakened and appear apathetic
• Many cannot stand without
support
• Look old
• Hair is thin, dry, and lacks
sheen
• Body temperature and blood
pressure are low
• Prone to dehydration,
infections, and unnecessary
blood clotting
Figure 6.17
Types of PEM: Marasmic Kwashiorkor
 Chronic deficiency in kilocalories
and protein
• Have edema in legs and arms
• Have a “skin and bones”
appearance
• With treatment the edema
subsides and appearance becomes
more like someone with marasmus

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Treatment for PEM
 Medical and nutritional treatment can dramatically reduce
mortality rate
 Should be carefully and slowly implemented
• Step 1 – Address life-threatening factors
- Severe dehydration
- Fluid and nutrient imbalances
• Step 2 – Restore depleted tissue
- Gradually provide nutritionally dense kilocalories and
high-quality protein
• Step 3 – Transition to foods and introduce physical
activity

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Quick Review
 High-protein diet may play a role in increasing risk of heart
disease, kidney problems, and calcium loss from bones
 Consuming too much protein from animal sources increase
saturated fat intake
 Too much protein can displace whole grains, fruits, and
vegetables, which have been shown to reduce many chronic
diseases
 Low-protein diet can lead to loss of bone mass
 PEM is caused by inadequate protein and/or kilocalorie
intake
• Kwashiorkor – severe protein deficiency
• Marasmus – severe kilocalorie deficiency

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Vegetarian Diet
 People choose vegetarian diets for a variety of reasons
• Ethical
• Religious
• Environmental
• Health

 Vegetarians must consume adequate amounts of a variety

of food and should plan meals well

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Potential Benefits, Risks of a Vegetarian Diet
 Benefits of a healthy vegetarian diet
• Reduced risk of
- Heart disease - Cancer
- High blood pressure - Stroke
- Diabetes - Obesity

 Potential risks of a vegetarian diet

• Underconsumption of certain nutrients
- Protein
- Vitamin B12

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Vegetarian Food Guide Pyramid

Figure 6.18
Soy
 Soy is increasing in popularity in the United States
• High-quality protein source
• Low in saturated fat
• Contains isoflavones
• Phytoestrogens
• May reduce risk of heart disease
• Some research suggests it may reduce the risk of cancer
• Some concern it may promote breast cancer

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Quick Review
 Vegetarian diets can be a healthy eating style that may help
reduce the risk of some chronic disease
 Some vegetarians abstain from all animal products
 Some vegetarians eat eggs and dairy in limited amounts
 Vegetarians must plan their diets carefully to meet their
nutrient needs, especially
• Protein • Riboflavin
• Iron • Vitamin B12
• Zinc • Vitamin A
• Calcium • Omega-3 fatty acids
• Vitamin D

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Putting It All Together
 Majority of daily kilocalories should come from
carbohydrate-rich foods
 Fat intake should be no more than about one-third of daily
kilocalories
 Protein should provide the rest of the daily kilocalories

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Putting It All Together
 Best plan for a healthful diet
• Eat an abundance of
- Grains (at least ½ whole grains)
- Vegetables
- Fruits
• Eat modest amounts of
- Commercially made bakery and snack items
- Vegetables with creamy sauces or added butter
- Sweets
• Choose low-fat dairy products, lean meat, poultry, and
fish to minimize the intake of heart-unhealthy saturated
fats

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