1. Topic 6: Protein & Amino acids Chris Blanchard
BMS208 Human Nutrition
Topic 6: Protein & Amino acids
Chris Blanchard

2. Learning objectives
Describe how the chemical structure of proteins differs from the structures of carbohydrates and fats.
List the 9 essential amino acids.
Trace the digestion of protein and list the enzymes needed to complete the process.
Explain the process used by the body to synthesize new proteins.
List the 8 major functions of protein in the body.
Describe nitrogen balance and provide examples of positive nitrogen balance, negative nitrogen balance, and equilibrium.
Describe deamination, where it occurs in the body, the products produced, and the fate of these products.

3. Learning objectives
Discuss the factors used to evaluate protein quality.
Describe the diseases that result from inadequate intake of protein and protein-kcalories.
Discuss the health effects of over-consumption of protein.
Calculate the protein needed daily using the RDA for protein.
Discuss the health risks of protein and amino acid supplements.
Define nutritional genomics and explain its potential uses in health care.

4. Proteins
Proteins are made from 20 different amino acids, 9 of which are essential.
Each amino acid has an amino group, an acid group, a hydrogen atom, and a side group.
It is the side group that makes each amino acid unique.
The sequence of amino acids in each protein determines its unique shape and function.

5. Amino acid structure

6. Amino acid structure

7. Amino Acids
Have unique side groups that result in differences in the size, shape and electrical charge of an amino acid
Nonessential amino acids, also called dispensable amino acids, are ones the body can create.
Nonessential amino acids include alanine, arginine, asparagine, aspartic acid, cysteine, glutamic acid, glutamine, glycine, proline, serine, and tyrosine.

8. Amino Acids
Essential amino acids, also called indispensable amino acids, must be supplied by the foods people consume.
Essential amino acids include histidine, isoleucine, leucine, lysine, methionine, phenyalanine, threonine, tryptophan, and valine.
Conditionally essential amino acids refer to amino acids that are normally nonessential but essential under certain conditions.

9. Peptides
Amino acid chains are linked by peptide bonds in condensation reactions.
Dipeptides have two amino acids bonded together.
Tripeptides have three amino acids bonded together.
Polypeptides have more than two amino acids bonded together.
Amino acid sequences are all different, which allows for a wide variety of possible sequences.

10. Peptides bonds

11. Protein Shapes Hydrophilic side groups are attracted to water.
Hydrophobic side groups repel water.
Coiled and twisted chains help to provide stability.

12. Protein Shapes

13. Protein Shapes

14. Protein Functions Some carry and store materials.
Some provide strength.
Some require minerals for activation (example: hemoglobin and the mineral iron).

15. Protein denaturation
Uncoiling of protein that changes its ability to function.
Proteins can be denatured by heat and acid.
After a certain point, denaturation cannot be reversed.

16. Digestion and Absorption
Stomach acid and enzymes facilitate the digestion of protein.
It is first denatured, then broken down to polypeptides.
The small intestine continues to break down protein into smaller peptides and amino acids so it can be absorbed.

17. Digestion In the Stomach Protein is denatured by hydrochloric acid.
Pepsinogen (a proenzyme) is converted into its active form pepsin in the presence of hydrochloric acid.
Pepsin cleaves proteins into smaller polypeptides.

18. Digestion In the Small Intestine
Proteases hydrolyze protein into short peptide chains called oligopeptides, which contain four to nine amino acids.
Peptidases split proteins into amino acids.

19. Absorption
Used by intestinal cells for energy or synthesis of necessary compounds
Transported to the liver
Taking enzyme supplements or consuming predigested proteins is unnecessary

20. Proteins in the Body
Proteins are versatile and unique. The synthesis of protein is determined by genetic information.
Protein is constantly being broken down and synthesized in the body.
Researchers measure nitrogen balance to study synthesis, degradation and excretion of protein.
Protein has many important functions in the body.
Protein can be used for energy if needed; its excesses are stored as fat.
The study of proteins is called proteomics.

21. Protein Synthesis
Synthesis is unique for each human being and is determined by the amino acid sequence.
Delivering the instructions through messenger RNA
Carries a code to the nuclear membrane and attaches to ribosomes
Presents a list to make a strand of protein
Transfer RNA lines up the amino acids and brings them to the messenger

22. Protein Synthesis
Sequencing errors can cause altered proteins to be made.
An example is sickle-cell anemia where an incorrect amino acid sequence interferes with the cell’s ability to carry oxygen.
Cells regulate gene expression to make the type of protein needed for that cell.
Epigenetics refers to a nutrient’s ability to activate or silence genes without interfering with the genetic sequence.

23. Roles of Proteins Building Materials for Growth and Maintenance
A matrix of collagen is filled with minerals to provide strength to bones and teeth.
Replaces tissues including the skin, hair, nails, and GI tract lining
Enzymes are proteins that facilitate anabolic (building up) and catabolic (breaking down) chemical reactions.
Hormones regulate body processes and some hormones are proteins. An example is insulin.

24. Enzymes

25. Roles of Proteins Regulators of Fluid Balance
Plasma proteins attract water
Maintain the volume of body fluids to prevent edema which is excessive fluid
Maintain the composition of body fluids

26. Roles of Proteins Acid-Base Regulators
Act as buffers by keeping solutions acidic or alkaline
Acids are compounds that release hydrogen ions in a solution.
Bases are compounds that accept hydrogen ions in a solution.
Acidosis is high levels of acid in the blood and body fluids.
Alkalosis is high levels of alkalinity in the blood and body fluids.

27. Roles of Proteins Transporters
Carry lipids, vitamins, minerals and oxygen in the body
Act as pumps in cell membranes, transferring compounds from one side of the cell membrane to the other

28. Roles of Proteins Antibodies
Fight antigens, such as bacteria and viruses, that invade the body
Provide immunity to fight an antigen more quickly the second time exposure occurs

29. Roles of Proteins Source of energy and glucose if needed Other Roles
Blood clotting by producing fibrin which forms a solid clot
Vision by creating light-sensitive pigments in the retina

30. Protein Metabolism Protein Turnover and the Amino Acid Pool
Protein turnover is the continual making and breaking down of protein.
Amino acid pool is the supply of amino acids that are available.
Amino acids from food are called exogenous.
Amino acids from within the body are called endogenous.

31. Protein Metabolism Nitrogen Balance
Zero nitrogen balance is nitrogen equilibrium, when input equals output.
Positive nitrogen balance means nitrogen consumed is greater than nitrogen excreted.
Negative nitrogen balance means nitrogen excreted is greater than nitrogen consumed.

32. Protein Metabolism
Using Amino Acids to Make Proteins or Nonessential Amino Acids
Cells can assemble amino acids into the protein needed.
Using Amino Acids to Make Other Compounds
Neurotransmitters are made from the amino acid tyrosine.
Tyrosine can be made into the melanin pigment or thyroxine.
Tryptophan makes niacin and serotonin.
Using Amino Acids for Energy and Glucose
There is no readily available storage form of protein.
Breaks down tissue protein for energy if needed

33. Protein Metabolism Deaminating Amino Acids
Nitrogen-containing amino groups are removed.
Ammonia is released into the bloodstream.
Ammonia is converted into urea by the liver.
Kidneys filter urea out of the blood.
Using Amino Acids to Make Fat
Excess protein is deaminated and converted into fat.
Nitrogen is excreted.

34. Protein in Foods
Eating foods of high-quality protein is the best assurance to get all the essential amino acids.
Complementary proteins can also supply all the essential amino acids.
A diet inadequate in any of the essential amino acids limits protein synthesis.
The quality of protein is measured by its amino acid content, digestibility, and ability to support growth.

35. Protein Quality Digestibility Depends on protein’s food source
Animal proteins are 90-99% absorbed.
Plant proteins are 70-90% absorbed.
Soy and legumes are 90% absorbed.
Other foods consumed at the same time can change the digestibility

36. Protein Quality Amino Acid Composition
The liver can produce nonessential amino acids.
Cells must dismantle to produce essential amino acids if they are not provided in the diet.
Limiting amino acids are those essential amino acids that are supplied in less than the amount needed to support protein synthesis.
Reference Protein is the standard by which other proteins are measured.
Based on their needs for growth and development, preschool children are used to establish this standard.

37. Protein Quality High-Quality Proteins Complementary Proteins
Contains all the essential amino acids
Animal foods contain all the essential amino acids.
Plant foods are diverse in content and tend to be missing one or more essential amino acids.
Complementary Proteins
Combining plant foods that together contain all the essential amino acids
Used by vegetarians

38. Protein Quality

39. Protein Quality
A Measure of Protein Quality - PDCAAS (protein digestibility-corrected amino acid score)
Compares amino acid composition of a protein to human amino acid requirements
Adjusts for digestibility

40. Protein in Foods Protein Regulation for Food Labels
List protein quantity in grams
% Daily Values is not required but reflects quantity and quality of protein using PDCAAS.

41. Health Effects and Recommended Intakes of Protein
Protein deficiency and excesses can be harmful to health.
Protein deficiencies arise from protein-deficient diets and energy-deficient diets.
This is a worldwide malnutrition problem, especially for young children.
High-protein diets have been implicated in several chronic diseases.

42. Health Effects and Recommended Intakes of Protein
Protein-Energy Malnutrition (PEM) – also called protein-kcalorie malnutrition (PCM)
Classifying PEM
Chronic PEM and acute PEM
Maramus, kwashiorkor, or a combination of the two

43. Protein-Energy Malnutrition
Marasmus
Infancy, 6 to 18 months of age
Severe deprivation or impaired absorption of protein, energy, vitamins and minerals
Develops slowly
Severe weight loss and muscle wasting, including the heart
< 60% weight-for-age
Anxiety and apathy
Good appetite is possible
Hair and skin problems

44. Protein-Energy Malnutrition
Kwashiorkor
Older infants and young children, 18 months to 2 years of age
Inadequate protein intake, infections
Rapid onset
Some muscle wasting, some fat retention
Growth is 60-80% weight-for-age
Edema and fatty liver
Apathy, misery, irritability and sadness
Loss of appetite
Hair and skin problems

45. Protein-Energy Malnutrition
Marasmus-Kwashiorkor Mix
Both malnutrition and infections
Edema of kwashiorkor
Wasting of marasmus

46. Protein-Energy Malnutrition
Infections
Lack of antibodies to fight infections
Fever
Fluid imbalances and dysentery
Anemia
Heart failure and possible death
Rehabilitation
Nutrition intervention must be cautious, slowly increasing protein.
Programs involving local people work better.

47. Health Effects of Protein
Heart Disease
Foods high in animal protein also tend to be high in saturated fat.
Homocysteine levels increase cardiac risks.
Arginine may protect against cardiac risks.

48. Health Effects of Protein
Cancer
A high intake of animal protein is associated with some cancers.
Is the problem high protein intake or high fat intake?
Adult Bone Loss (Osteoporosis)
High protein intake associated with increased calcium excretion.
Inadequate protein intake affects bone health also.

49. Health Effects of Protein
Weight Control
High-protein foods are often high-fat foods.
Protein at each meal provides satiety.
Adequate protein, moderate fat and sufficient carbohydrate better support weight loss.
Kidney Disease
High protein intake increases the work of the kidneys.
Does not seem to cause kidney disease

50. Recommended Intakes of Protein
10-35% energy intake
Protein RDA
0.8 g/kg/day
Assumptions
People are healthy.
Protein is mixed quality.
The body will use protein efficiently.

51. Recommended Intakes of Protein
Adequate Energy
Must consider energy intake
Must consider total grams of protein
Protein in abundance is common in first world countries

52. Protein and Amino Acid Supplements
Many reasons for supplements
Protein Powders have not been found to improve athletic performance.
Whey protein is a waste product of cheese manufacturing.
Purified protein preparations increase the work of the kidneys.

53. Protein and Amino Acid Supplements
Amino Acid Supplements are not beneficial and can be harmful.
Branched-chain amino acids provide little fuel and can be toxic to the brain.
Lysine appears safe in certain doses.
Tryptophan has been used experimentally for sleep and pain, but may result in a rare blood disorder.

54. Nutritional Genomics

55. Nutritional Genomics
In the future, genomics labs may be used to analyze an individual’s genes to determine what diseases the individual may be at risk for developing.
Nutritional genomics involves using a multidisciplinary approach to examine how nutrition affects genes in the human genome.

56. A Genomics Primer
Human DNA contains 46 chromosomes made up of a sequence of nucleotide bases.
Microarray technology is used to analyze gene expression.
Nutrients are involved in activating or suppressing genes without altering the gene itself.
Epigenetics is the study of how the environment affects gene expression.
The benefits of activating or suppressing a particular gene are dependent upon the gene’s role.

57. A Genomics Primer

58. Genetic Variation and Disease
Small differences in individual genomes
May affect ability to respond to dietary modifications
Nutritional genomics would allow for personalization of recommendations.
Single-Gene Disorders
Mutations cause alterations in single genes.
Phenylketonuria is a single-gene disorder that can be affected by nutritional intervention.

59. Genetic Variation and Disease
Multigene Disorders
Multiple genes are responsible for the disease.
Heart disease is a multigene disorder that is also influenced by environmental factors.
Genomic research may be helpful in guiding treatment choices.
Variations called single nucleotide polymorphisms (SNPs) may influence an individual’s ability to respond to dietary therapy.

60. Clinical Concerns
An increased understanding of the human genome may impact health care by:
Increasing knowledge of individual disease risks
Individualizing treatment
Individualizing medications
Increasing knowledge of nongenetic causes of disease
Some question the benefit of identifying individual genetic markers.
Even if specific recommendation can be made based on genes, some may choose not to follow recommendations.