Chemistry of Proteins Chapter 6

Proteins are made of many Amino Acids (AA) connected together

Proteins

Amino Acids
!!All
!! !! !! !! !!

Amino Acid Structure

AAs have the same basic structure

Central carbon (C) Hydrogen (H) Acid (COOH) Amino Group (NH2) Exception: side group or side chain R

!!Differences !!Around

in the side group are what make each AA unique 20 different AAs

Amino Acids

Proteins
!! Consist

The area in white in each of the boxes above are the R groups referred to previously that makes each amino acid unique.

of AAs linked together in different combinations !! Sequence of AAs determines the conformation (3-D structure) which dictates the type and function of the protein !! AAs are connected to each other through a peptide bond
!! condensation

reaction

Amino acids connected together through a peptide bond

Insulin

=BOND CONNECTS ACID END (1) WITH THE AMINO ENDOF 2

Insulin is a peptide (protein) hormone made up of amino acids. The order of the amino acids dictates the structure of insulin and the structure of insulin dictates its function. One amino acid out of sequence could possibly make insulin nonfunctional.

AA NONESSENTIAL ESSENTIAL CONDITIONALLY ESSENTIAL

AA CHAINS DIPEPTIDE TRIPEPTIDE POLYPEPTIDE AA SEQUENCE VARIETY OF POSSIBLE SEQUENCE AA SHAPES PROTEIN FUNCTIONS BASED ON THE SHAPE (HOLLOW BALLS, LONG (TENDONS) HEMOGLOBIN (LARGE, GLOBULAR-CARRIES RBC) IS MADE OF 4 POLYPEPTIDE CHAINS PROTEIN DENATURATION (HEAT, ACID, ETC) UNCOIL, LOSE SHAPES AND FUNCTIONS

2001 Brooks/Cole, a division of Thomson Learning, Inc. Thomson Learning is a trademark used herein under license.

Digestion of Proteins
-Breaking the large protein molecule down to smaller subunits
!! Amino

Acids

Mouth
Only crushing and moistening occurs

Figure 6-5 The structure of Hemoglobin

Digestion
Stomach
- Chemical breakdown (hydrolysis) - Protein loses its 3-D structure (denaturation) due to the acidic environment (HCl) - HCl converts inactive enzyme pepsinogen to active form pepsin - Enzymatic breakdown peptidase pepsin

Figure 6-6 Protein digestion in the GI Tract

Digestion
Small intestine - Pancreatic and intestinal proteases
!!Enzymes

Question

specific for certain peptide bonds !!Proteins are broken down into:
!! !! !!

oligopeptides dipeptides tripeptides

Given that insulin is a protein what would its fate be if it were taken orally?

Absorption
Intestinal cells absorb single amino acids, diand tri-peptides !! AAs must pass through the cell membrane, through the cell and then through the cell membrane again !! Absorption occurs through transporters specific for certain AAs !! Transporters located in cell membrane !! Absorption requires energy
!!

Absorption of Nutrients Active Transport

Essentiality of Amino Acids

Essential
Amino acids that cannot be made by the body and therefore must be supplied by the diet

Essentiality of Amino Acids

Nonessential amino acids
- Amino acids that can be made by the body

Conditionally essential amino acids

- AAs that are normally made providing the precursors are available

Protein in the Body

Protein Synthesis Transcription: DNA !! RNA
- Taking the information from DNA and transcribing it into RNA

Protein Synthesis

Translation: RNA !! Protein

- Taking the information from RNA and translating it into an amino acid

The Site of Reactions - Cells

2001 Brooks/Cole, a division of Thomson Learning, Inc. Thomson Learning is a trademark used herein under license.

2001 Brooks/Cole, a division of Thomson Learning, Inc. Thomson Learning is a trademark used herein under license.

Figure 6-7 Protein synthesis

Fig 7-4 Page 207

Errors in Protein Synthesis

Example: Sickle cell anemia
- One AA is wrong causing the structure of hemoglobin structure to change resulting in a dysfunctional protein

Roles of Proteins
1. Building materials Growth and maintenance
- Muscle tissue - Bone tissue - Blood - Skin - Intestinal cells

Repair
- Clotting factors
Fig. 6-8 Page 175

Roles of Proteins-Building materials

Replacement
- Red blood cells
Life span of ~120 days

Roles of Proteins
2. Enzymes
- Enable vital reactions to occur
Example: Digestive enzymes

- Insulin
Half-life of 6-10 minutes

3. Hormones
- Compounds made in one cell or organ that elicit effects upon other organs
Examples: Insulin and glucagon

- Protein turnover
Continuous breakdown and synthesis

Enzymes
Each enzyme facilitates a specific reaction

Roles of Proteins
4. Regulate fluid balance
- Proteins affect osmotic pressure Osmosis: Water will move from and area of low solute concentration into an area of higher solute concentration. Solutes can be proteins, salt, etc. If the concentration of proteins in the blood decreases, perhaps due to malnutrition, the effective solute concentration in the interstitial space has increased. Water will leave the blood vessels and enter into the interstitial space resulting in edema (swelling).
Fig. 6-9 Page 177

Fluid Balance
If the concentration of proteins in the blood decreases, perhaps due to malnutrition, the effective solute concentration in the interstitial space has increased. Water will leave the blood vessels and enter into the interstitial space resulting in edema (swelling).

Roles of Proteins
5. Regulates acid-base balance
- Proteins(-) attract hydrogen(+)

6. Transporters and receptors

- In blood proteins transport:
!! Glucose !! Water !! Fat,

insoluble compounds steroids, hormones, vitamins glucagon, estrogen

- Hormone receptor
!! Insulin,
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Transport Proteins (Na/K pump)

Roles of Proteins
7. Antibodies
- Specifically attack foreign bodies

8. Other roles
- Neurotransmitters - Blood clotting - Visual pigments

Fig. 6-10 Page 179

Protein Metabolism
Protein turnover
- Continuous breakdown and synthesis

Protein Metabolism
Nonessential amino acids
!!

Nitrogen balance
a. Balance: intake = output - Normal losses include: urine, feces, sweat,
skin, hair

Some can be made from other amino acids to support protein synthesis

b. Negative balance: intake < output

- Nitrogen consumed is less than that lost - " loss due to stress or injury

If there is a deficiency
!! Body protein will be broken down to obtain necessary amino acids

c. Positive balance: intake > output - Nitrogen consumed is more than that lost

Protein Metabolism
Using amino acids to make glucose for energy
1. Deamination a. Removal of the amino group (N) 2. Carbon skeleton then used to make glucose (gluconeogenesis) b. used for energy c. excess used to make fat (lipogenesis)

Protein in Foods

Protein quality
1. Complete protein
Contains all essential amino acids in amounts we require
!! !!

Protein quality
2. Incomplete protein
Lack limiting amino acid
- One essential amino acid that is not present in sufficient amounts

support growth maintain adults protein

Examples:
- Cereals # lysine - Legumes # methionine

Example:
- Animal proteins - Egg protein is reference protein

Must be supplied by another food complementary protein

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Complimentary Proteins
Combining incomplete protein sources

Measurement of protein quality

Chemical scoring
- Amino acid profile compared to reference protein (egg) Example: If valine is present at 70% of egg value then the score is 70

Black beans & rice bread

Peanut butter &

Measurement of protein quality

Biological value (BV) - Measure of nitrogen retained from a
given amount absorbed

Health Effects and Recommended Intakes of Protein

Protein efficiency ratio (PER)

- Measure of how well a protein supports weight gain (in growing rats)
- Used as index for proteins for infants

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PROTEIN REQUIREMENTS ADULTS: equal balance CHILDREN, infants, pregnant and lactating women RDA (Recommended Levels of Intake) 0-6 mo 2.2 6mo-1 year 1.6 1 to 3 years 1.2 4 to 6 years 1.1 7 to 10 years 1.0 11-14 years 1.0 15-18 years (males) 0.9 15-18 years (males) 0.8 Pregnancy +10, +15g/d Lactation +15, +12 g/d

Recommended Intake of Protein

RDA: 0.8 g/kg body weight or 0.36 g/lb
(~15% of caloric intake)
19-24 AGE GROUP ADULT MALES ADULT FEMALES >25 YEARS OLD MALES FEMALES 63g/d 50g/d 58 g/d 46 g/d

TYPICAL INTAKES IN U.S. ADULT MEN ADULT WOMEN 92 g/d 60 g/d

FOOD SOURCES OF PROTEINS CONTRIBUTIONS BY FOOD GROUPS: MEATS, FISH, EGGES 47% DAIRY PRODUCTS 21% CEREALS 19% FRUITS AND VEGETABLES 7% LEGUMES 5.4%

Protein adequacy is NOT a problem in the US

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Animal versus vegetable protein

!! Vegetable

protein lowers blood cholesterol !! Vegetables are low in fat, high in fiber !! Animal protein is higher quality

SOCRATES, PLATO, EINSTEIN, LEONARDO DA VINCI, SHAKESPEARE, DARWIN, GANDHI WHAT DID THEY HAVE IN COMMON?

PROTEIN DEFICIENCIES WHO will have problems getting enough protein? VEGETARIANS Lacto-ovo Lacto Vegan Will Eat dairy, eggs dairy Wont eat meat meat, eggs

HOW MANY VEGETARIANS ARE IN THE US?

avoids foods of animal origin: meat dairy, eggs

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Protein-energy malnutrition (PEM)

Problem in developing countries

Types of PEM
1. Marasmus (severe-chronic PEM)
- severe deprivation or malabsorption of protein and calories

Deprivation of protein, calories or both

- Most widespread form of malnutrition
!! poor !! wasting

growth in children in adults

2. Kwashiorkor (acute PEM)

- inadequate protein intake or infections

- Children mostly afflicted

Marasmus (dying away)

!! Chronic

Kwashiorkor (the evil spirits that

!! Sudden !! Children !! Some

food deprivation !! Children 6-18 mo. !! Impairs brain development & learning !! Muscle wasting, including heart !! Severe weight loss

infects the first child when the second is born) 1-3 years weight loss !! Edema !! Enlarged fatty liver !! Hair: dry, brittle, changes color

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Health Effects of ! Protein

1. Contributes to obesity
- High protein foods are often high fat foods - Excess protein often = excess fat

DO ATHLETES NEED MORE PROTEIN?

PROTEIN REQUIREMENTS FOR ATHLETES RISK OF SUPPLEMENTS

2. Promotes calcium loss from body

- 2x increase in protein intake ! 50% increase in urinary calcium loss

3. Stresses kidney and liver

Misconception: Extra protein from foods or use of protein supplements will help increase muscle strength.

MUSCLE WORK BUILDS MUSCLE; PROTEIN SUPPLEMENTS DO NOT ATHLETES NEED A WELL BALANCED DIET THAT PROVIDES SUFFICIENT DIETARY PROTEIN AND ADEQUATE FOOD ENERGY

!!

Protein is made of small building units called amino acids. In the body amino acids are used to make structural tissue (muscle, bone, skin), enzymes, some of the hormones, and neurotransmitters. Even though amino acids are critical for making these very important body protein elements, extra amounts of amino acids will not build muscle strength. If more protein is provided to the body than needed, the extra will be used as energy or stored as fat. Training and hard work on the muscles are responsible for building strength.

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Misconception: Because of exercise, athletes need to reinforce their diets with extra protein.
!!

Misconception: Since muscle is made of protein, athletes should take protein supplements.
!! Even

The usual recommendation for protein is to provide approximately 0.8 gram of protein per kilogram of body weight for a normal, healthy adult. Children and adolescents who are growing have a slightly higher need for protein than adults. Athletes, due to their regular daily activity that can affect muscle maintenance and repair, may need slightly more protein than non-exercisers. Research suggests endurance athletes may need from 1.2 to 1.4 g protein per kilogram body weight. Athletes who are involved in very intense strength training may need up to 1.7 protein per kilogram of body weight. In the United States, diets contain enough protein to meet these levels, as long as enough energy is consumed to protect protein from being used as an energy source.

if an athlete's need for protein is slightly greater than normal needs, protein supplements are not necessary.

!! Protein

supplements can be helpful in certain medical situations. For example, an athlete with anorexia may be more willing to consume a protein shake than eat tuna, cottage cheese or chicken. Patients with cancer or AIDS often benefit from protein supplements if they are unable to eat well.

!! NO

scientific evidence supports the idea the protein or amino acids in supplements are in any way superior to the protein from eggs, milk, lean meats, fish, soy or other ordinary foods.

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Is more better?
Eating more than the recommended protein intake offers no benefits. Apart from being costly, a protein-based diet commonly displaces important carbs from the diet. That is, if you have an omelet and a protein shake for breakfast instead of cereal with banana, you'll consume fewer carbs to fuel your muscles properly.
!! Carbs

are the primary fuel for athletes who do muscle-building resistance exercise. Once your muscles become carb-depleted, fatigue sets in and your workout is over. Your diet should provide extra carbs, not extra protein

Misconception: Athletes should get extra protein for insurance. After all, there's no
!! If

you consume too much protein from supplements, you may also fail to invest in optimal health. Displacing natural foods with engineered foods (such as protein supplements) limits your intake of the vegetables, fruits, grains, fiber, phytochemicals, natural vitamins and other health-protective nutrients that Nature puts in whole foods.

danger in getting too much protein

!!

There are slight risks associated with getting too much protein. Extra protein makes more work for the liver and kidneys, which have to handle the extra nitrogen from the amino acids. This can lead to an increased risk for liver and kidney problems in later years. Also, more water will be needed to help the kidneys handle the workload of excreting nitrogen as urea so there is a greater risk for dehydration.

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LYSINE MIGHT BE HELPFUL IN CONTROLLING HERPES SIMPLEX-RELATED INFECTIONS (HSV)

IT INHIBITS THE GROWTH OF HSV BY KNOCKING OUT ARGININE

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