Chapter 7 proteins
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Chapter 7: Proteins. Major building blocks. Much of the body is made of protein 17% of total body weight Mostly muscle tissue/lean body tissue Contain nitrogen (amino acids) What do amino acids contain?. R group Acid group

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Chapter 7: Proteins

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Chapter 7 proteins

Chapter 7: Proteins


Major building blocks

Major building blocks

  • Much of the body is made of protein

    • 17% of total body weight

    • Mostly muscle tissue/lean body tissue

  • Contain nitrogen (amino acids)

    • What do amino acids contain?


Amino acid

R group Acid group

Amine group

Amino Acid

NH2 O

R C C OH

H


Chapter 7 proteins

Essential AA

Nonessential AA

Histidine

Alanine

Isoleucine

Arginine

Leucine

Asparagine

Lysine

Aspartic Acid

Methionine

Cysteine

Phenylalanine

Glutamic acid

Threonine

Glutamine

Tryptophan

Glycine

Valine

Proline

Serine

Tyrosine


Amino acids

Amino acids

  • 9 essential amino acids

    • Cannot be made by the body, must come from diet

    • Found in foods that come from animal sources

    • Plant proteins may be combined to make complete proteins containing these essential amino acids

  • 11 non-essential amino acids

    • Body can make these amino acids from essential amino acids or as long as there is sufficient nitrogen


Making an essential amino acid

Making an Essential Amino Acid

Phenylalanine Tyrosine

(Essential AA)phenylalanine hydroxyase (Nonessential AA)


Phenylketonuria

Phenylketonuria

Phenylalanine Tyrosine

(Essential AA)phenylalanine hydroxyase(Nonessential AA)

“ MISSING; LACKING”

Control Intake Becomes essential


Synthesis of nonessential amino acids

Synthesis of Nonessential Amino Acids

  • Transamination

    • Addition of an amino grp to a carbon skeleton to form a new non-essential amino acid.

  • Deamination

    • The removal of an amino group from an amino acid

    • Occurs during protein metabolism


Synthesis of nonessential amino acid

Synthesis of Nonessential Amino Acid

Transamination and Deamination


Functions of proteins in our diet

Functions of Proteins in Our Diet

  • Provide the 9 essential amino acids

  • Provide the nonessential amino acids or nitrogen to make the nonessential amino acids

  • Protein have many functions

    • Regulate and maintain body functions

    • Cell repair

    • Supply energy (4 kcal/g)


Quality of protein

Quality of Protein

  • High quality protein or complete protein

    • Contains ample amount of all 9 essential AA

    • Animal proteins: contain all EAA in sufficient quantities

  • Low quality protein

    • Deficient or low in one or more essential AA

    • Plant proteins (except Soybean)

  • All-or-none principle

    • Diet must supply all 9 EAA for protein synthesis


Limiting amino acid

Limiting Amino Acid

The EAA in lowest conc in a diet relative to body needs. C is the limiting amino acid in this example

CCCCC

AAAAAAAA CAR CAR CAR

RRRRRR CAR CAR

R

A A A


Complementary proteins

Complementary Proteins

Food 1 Food 2

CC CCCC

AAAA AA CAR CAR CAR

RRR RRR CAR CAR CAR


Complementary protein table 7 2

Complementary Protein: (Table 7.2)

  • Mixed diets provides high quality protein because a complimentary protein pattern results

  • Essential amino acids must be 40% of total protein intake for infants and pres-school children

    • Diets need careful planning

  • For adults; EAA -11% of total pn intake


Complementary protein table 7 21

Complementary Protein: (Table 7.2)

Beans (legumes)

  • GrainsNuts/seeds

  • Vegetables


Protein organization

Peptide bond

Dipeptide

Tripeptide

Oligopeptide

Protein Organization

SH SH

CH2 CH2

H O CH H2O H O CH

H N C OH H N C OH H N C N C OH

CH H O CH H O

CH3 H2O CH3


Protein synthesis

Protein Synthesis


Turnover and metabolism

Turnover and Metabolism


Protein turnover

Protein turnover

  • Protein turnover – the degradation and synthesis of endogenous protein.

  • When proteins break down, they free amino acids to join the general circulation…what happens next?

    • Recycled to make new proteins (or other Ncontaining compounds) OR

    • – Nitrogen is removed and remaining part of amino acid is used for energy (Deamination: NH2 is removed to make urea)


Summary of protein synthesis in the body

Summary of Protein Synthesis inthe Body

  • • DNA in nucleus of cell acts as a template

  • • mRNA from cytoplasm of cell enters nucleus

  • • Portion of DNA unwinds and mRNA matches up with it to transcribe the pattern

  • • mRNA leaves nucleus and goes to cytoplasm of cell

  • • mRNA hooks onto ribosomes

  • • tRNA brings in single amino acids one-at-a-time

  • • Amino acid placed on mRNA where so directed by template (called translation)

  • • Amino acids enzymatically joined into a protein

  • • Protein is released into cell fluid


Chapter 7 proteins

  • When an essential amino acid (EAA) is missing, protein synthesis stops, and the remaining amino acids are deaminated and the nitrogen is excreted in the urine.

  • Vegetarians must pay CLOSE attention to protein complementation so as to not be deficient in any EAA!


Protein organization1

Protein Organization

  • Primary structure

    • Sequence of AA; affects protein’s shape

    • Related to sickle cell anemia (fig 7.3)

  • Secondary structure

    • Bends and folds held together by bonds

    • Formed by interactions of AA at various positions

  • Tertiary structure

    • 3-D shape: affects function of protein

  • Quaternary structure

    • 2 or more proteins interacting together


Denaturation of proteins

Heat/acid/alkaline/enzymes

Result in alteration of the protein’s three dimensional structure

Denaturation of Proteins


Digestion of protein in the stomach

Digestion of Protein in the Stomach

  • Proteins are denatured by the cooking and the stomach acid

  • Gastrin (hormone) stimulates the release of pepsinogen and acid from cells in the stomach

  • Pepsinogen is converted to pepsin by the acid in the stomach

  • Pepsin (an enzyme produced in the stomach) breaks down proteins into peptones


Digestion of protein in the small intestine

Digestion of Protein in the Small Intestine

  • Partially digested pns from stomach stimulate the release of CCK (cholesystokinin)

  • Causes pancreas to release the protein splitting enzymes: trypsin, chymotrypsin, and carboxypeptidase into the duodenum

  • The enzymes will break peptones into smaller peptides and amino acids

  • Peptides and amino acids are ready for absorption


Protein absorption fig 7 7

Protein Absorption (fig 7.7)

  • Active absorption

  • Whole proteins are broken down at the microvilli surface and within the absorptive cells

  • Whole proteins are eventually broken down to amino acids

  • Many different amino acid transport mechanisms

  • Amino acids are sent to the liver via portal circulation


Chapter 7 proteins

  • Protein Digestion and Absorption

  • Mouth

    • – no enzymatic digestion taking place; mechanical breakdown of proteins taking place

  • Stomach

    • HCl acid uncoils the large protein molecule so that Pepsin can begin to break the protein chain apart into smaller polypeptides, tripeptides, and dipeptides

    • Gastrin is released in the stomach to stimulate HCl acid production


Protein digestion absorption cont

Protein Digestion &Absorption Cont.

  • • Small Intestine

    • In the lumen, pancreatic and intestinal proteases break polypeptides into smaller tripeptides, dipeptides, and amino acids

    • At the brush border, intestinal tripeptidases and dipeptidases break down the tripeptides and dipeptides, respectively into amino acids for absorption

    • Note: these enzymes are “amino-acid” specific

    • Amino acids are absorbed into blood stream

      • most of the absorption takes place in the lower part of the small intestine


Functions of proteins

Functions of Proteins

  • Building blocks of body components

    • Muscle, connective tissue, mucus, blood clotting factors, bone,

    • Collagen, actin, myosin, hemoglobin, keratin

  • Maintain fluid balance

    • Albumins and globulins – blood proteins

    • Prevent excessive build up of fluid in the extracellular spaces

    • Reduces risks of edema

  • Contribute to acid/base balance

    • Maintenance of normal pH in blood

    • Act as buffers: regulate ion concentration blood and cells


Functions of proteins1

Functions of Proteins

  • Building blocks for hormones and enzymes

  • Immune function: antibodies

    • Lack of protein leads to anergy: reduced immune function

  • Gluconeogenesis

    • Formation of glucose

  • Energy yielding


Functions of proteins in the body

Functions of Proteins in theBody

  • Growth and Maintenance (collagen, muscle)

  • Formation of enzymes

  • Fluid balance – proteins attract water

  • Acid/base balance – act as buffers

  • Antibody formation

  • Hormone synthesis

  • Act as transport protein

  • Blood clotting – fibrin, collagen

  • Vision – opsin

  • Stored as fat if consumed in excess!


Measuring protein utilization and nitrogen balance fig 7 9

Measuring protein utilization and nitrogen balance (fig 7.9)

  • Protein not used is deaminated

    • Nitrogen is excreted in urine

    • 16% of protein molecule is N

  • Normally N intake = N out

  • Positive N balance : N in> N out

    • Growth, pregnancy, building muscles

  • Negative N balance

    • Wasting of body tissues

    • Loss of weight


Rda for protein

RDA for Protein

  • Promotes equilibrium

  • 0.8 gm of protein / kg of healthy body weight

    154 lb. = 70 kg

    2.2 kg/lb.

    70 kg x 0.8 g protein = 56 g protein

    kg healthy body wt


Rda for protein1

RDA for Protein

  • Increased by ~10-15 gm /day for pregnancy

  • Endurance athletes may need 1.5 - 2 gm/kg healthy weight

  • About 8-10% of total kcals

  • Most of us eat more than the RDA for protein

  • Excess protein cannot be stored as protein

  • The Food and Nutrition Board does not support any higher needs


Is a high protein diet harmful

Is a High-Protein Diet Harmful?

  • Likely to limit fruits and veg. and decrease fiber, vitamins, phytochemicals

  • Intake of animal protein increases risk for heart disease (high in saturated fat)

  • Excessive intake of red meat is linked with colon cancer

  • Burden on the kidney; need additional fluid to secrete N. may result in dehydration

  • Increase calcium loss

  • National Academy of Sciences recommends no more than 2 x RDA for protein


Individual amino acid aa supplement

Individual Amino Acid (AA) Supplement

  • Supplement may cause imbalances and toxicity (especially with methionine and tyrosine)

  • Body is designed to handle whole proteins

  • Supplement can overwhelm the absorptive mechanism

  • Excess of one AA can hamper absorption of other AAs


Vegetarian

Vegetarian

  • Without animal proteins, a diet can be deficient in essential amino acids –

    • Complete protein (animal) –

      • contains all of the amino acids essential in human nutrition in amounts adequate for human use

    • Incomplete protein (plant) –

      • limiting amino acid -EAA in the shortest supply, relative to the amounts needed for protein synthesis

  • Complementary proteins –

    • proteins that have different amino acid profiles, but when put together, resemble that of a complete protein source


Types of vegetarians

Types of Vegetarians

  • Semi-vegetarian –

    • some animal products, included in diet such as poultry and fish

  • Lactovegetarian –

    • will consume milk products in the diet

  • Ovo-vegetarian –

    • will consume eggs in the diet

  • Lacto-Ovo vegetarian

    • – will consume milk and eggs in the diet

  • Strict Vegetarian (vegan)

    • – no animal sources consumed, only foods of plant origin


Protein complementation

Protein Complementation

  • Combine cereal grains + legumes

  • Combine legumes + seeds & nuts

  • Rice + Beans

  • Peanut butter + Bread

  • Chili + Cornbread

  • Split pea soup + Sesame crackers


Protein sources

Protein Sources

  • Supplies protein in abundance:

    • Meats

    • Milk and dairy products

  • Supplies a moderate amount of protein:

    • Vegetables

    • Breads & Cereals

  • Supplies NO protein:

    • Fruits

    • Fats


Vegetarianism plant protein

Vegetarianism: Plant Protein

  • Somewhat less efficient (than animal protein)

  • No cholesterol and low in saturated fat

  • High in (soluble) dietary fiber, phytochemicals

  • Lacking in one or more essential amino acid


Soy protein

Soy Protein

  • Similar to animal protein (used in school lunches)

  • High in linoleic & a-linolenic acid

  • Contains Ca for bone health

  • Lowers blood cholesterol

  • Contains isoflavones (genistein and diadzein)

    • plantlike estrogen

  • Sources: tofu, soy milk, soy flour, tempeh, miso

  • Recommend 2-4 servings a week

  • Not recommended for women WITH breast cancer (or family history)


Evaluation of protein quality

Evaluation of Protein Quality

  • Ability to support body growth and maintenance

  • Measured under the condition that the amount of protein consumed is < body’s needs

  • Protein exceeding this amount becomes less efficient

  • Egg protein – has the highest quality protein; used as the “standard” from which all proteins in food are measured.


Biological value

Biological Value

  • Biological Value – the amount of protein nitrogen that is retained for growth and maintenance,

  • expressed as a percentage of the protein nitrogen that has been digested and absorbed; a measure of protein quality

  • Measure protein (AA) retention

Nitrogen retained

Nitrogen absorbed

BV =

X 100


Protein efficiency ratio

Protein Efficiency Ratio

  • Used by FDA to set standards for baby food

  • Compares the weight gained in a growing rat after 10 days or more eating a standard amount of protein

  • Measures BV (protein retention)

PER =

Gram weight gain

Gram protein consumed


Chemical score of protein

Chemical Score of Protein

  • Amount of each essential AA in a gram of protein in the food divided by an “ideal” amount for that essential AA

  • The lowest AA score is the C.S. for that food

Chem. Score

Mg of ess. AAn per gm of protein

Required mg needs of the ess. AAn per gm of protein

=


Protein digestibility corrected aa score pdcaas

Protein Digestibility Corrected AA Score (PDCAAS)

  • Most widely used (on food labels)

  • Maximum value is 1.0 (= milk, eggs, soy protein)

    PDCAAS = Chem. Score x (~0.9-1.0)

    Range of digestibility of that

    protein


Malnutrition

Malnutrition

  • Protein-Energy Malnutrition

  • Marasmus: disease of starvation

    • Seen in hospitalized patients

  • Kwashiorkor

    • Protein Malnutrition


Kwashiorkor

Kwashiorkor

  • Low protein density diet

  • Energy needs are marginally met

  • Signs and symptoms:

    • Apathy, listlessness, failure to grow, poor weight gain, change in hair color, nutrient deficiency, flaky skin, fatty infiltration in the liver, massive edema in the abdomen and legs


Marasmus

Marasmus

  • Starving to death

  • Insufficient protein, energy, nutrients

  • “skin and bones” appearance

  • Little or no subcutaneous fat

  • Reduce brain growth


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