Clinical Nutrition & Diet Therapy (PHAR322)

Proteins:
The Amino Acids - Course: Chapter 3
- Book Chapter 6
TOPICS:
* Part One:
- Structure & Classification of proteins & amino acids
- Digestion and absorption

* Part Two:
- Roles of protein

* Part Three:
- Protein quality

* Part Four:
- Recommended intake of proteins
- Protein and amino acid supplements
Part One:
- Structure & Classification of proteins & amino

acids (AA)

- Digestion and absorption

 Structure and Classification of proteins and AA
* Chemically:
-Proteins contain the same atoms as carbohydrates and lipids, carbon (C), hydrogen (H), and
oxygen (O)
But, proteins also contain nitrogen (N) atoms, and these nitrogen atoms give the name amino
(nitrogen containing) to the amino acids.

- Amino Acids have the same basic structure: a central carbon (C) atom, with a hydrogen atom
(H), an amino group (NH ), and an acid group (COOH) attached to it, and a fourth site that
2

distinguishes each amino acid from the others called the side chain or side group.

AA chemical structure
* This side group makes protein more complex compared to polysaccharides, for example a
polysaccaride is made of thousand units of the same glucose molecule, on the other hand a protein is
made up of about 20 different AA.
Note: The simplest amino acid, glycine, has a hydrogen atom as its side group.
A slightly more complex amino acid, alanine, has an extra carbon with three hydrogen
atoms. Other amino acids have more complex side groups.
Thus, although all amino acids share a common structure, they differ in size, shape,
electrical charge, and other characteristics because of differences in these side groups.
 Conditionally Essential AA

* Sometimes a nonessential amino acid becomes essential under special circumstances.

Eg: the body normally uses the essential amino acid phenylalanine to make tyrosine (a nonessential amino acid).

- But if the diet fails to supply enough phenylalanine, or if the body cannot make the conversion for some reason (as happens in the
inherited disease phenylketonuria “PKU”), then tyrosine becomes a conditionally essential amino acid.
 Proteins

* Cells link amino acids end-to-end in a variety of sequences to

form thousands of different proteins. A peptide bond unites each
amino acid to the next.

* Two amino acids bonded together form a dipeptide, and by

another such reaction, a third amino acid can be added to the chain
to form a tri-peptide. As additional amino acids join the chain, a
polypeptide is formed.
 The Formation of a Complex Protein Structure
1. Amino Acid Sequence (Primary Structure): The primary structure of a protein is determined by the sequence of amino
acids.

The first AA might be the amino acid methionine, the second might be an alanine, the third might be a glycine, the fourth a
tryptophan, and so on. Unlike Polysaccharides, all forming molecules are glucose.

2. Polypeptide Shapes (Secondary Structure): The secondary structure of proteins is determined not by chemical bonds as
between the amino acids but 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 into a pleated sheet. These shapes give proteins strength and rigidity.
 The Formation of a Complex Protein Structure, Cont.
3. Polypeptide Tangles (Tertiary Structure): 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
* Eg. Disulfide bridges in insulin determine its tertiary structure

Multiple Polypeptide Interactions (Quaternary Structures): Some polypeptides are functioning

proteins just as they are; others need to associate with other polypeptides to form larger working
complexes. The quaternary structure of proteins involves the interactions between two or more
polypeptides. One molecule of hemoglobin
- Protein Denaturation: When proteins are subjected to heat, acid, or other conditions that disturb
their stability, they undergo denaturation that is, they uncoil and lose their shapes and, consequently,
also lose their function, and at a certain point, denaturation is irreversible.
Examples: Hardening of an egg when it is cooked, the stiffening of egg whites when they are whipped.

* In the body, proteins are denatured when they are exposed to stomach acid.
 Protein digestion
* When we eat foods containing protein,
enzymes break the long polypeptide strands
into shorter strands, the short strands into
tripeptides and dipeptides, and, finally, the
tripeptides and dipeptides into amino acids.

* Proteins are crushed and moistened in the

mouth, but the real action begins in the
stomach.
 Protein digestion Cont.
* In the Stomach:

- The major event in the stomach is the partial breakdown (hydrolysis) of proteins.

a. Hydrochloric acid:

[Link] (denatures) each protein’s tangled strands so that digestive enzymes can
attack the peptide bonds.

2. Converts the inactive form of the enzyme pepsinogen to its active form, pepsin.

b. Pepsin (gastric enzyme):

1. Cleaves proteins “large polypeptides” into smaller polypeptides and some amino
acids.

Note: Inactive form of an enzyme is called a zymogen

 Protein digestion Cont.

* When polypeptides enter the small intestine, several pancreatic

and intestinal proteases hydrolyze them further into short peptide
chains, tripeptides, dipeptides, and amino acids.

* Then peptidase enzymes on the membrane surfaces of the

intestinal cells split most of the dipeptides and tripeptides into single
amino acids. Only a few peptides escape digestion and enter the
blood intact.
 Protein Absorption

* A number of specific carriers transport amino acids (and some dipeptides and tripeptides)

into the intestinal cells.

- Once inside the intestinal cells, amino acids may be used for energy or to synthesize needed

compounds.

- Amino acids that are not used by the intestinal cells are transported across the cell membrane

into the surrounding fluid where they enter the capillaries on their way to the liver.
 Part Two:
- Roles of protein
 Roles of protein in the human body
* When ever the body is growing, repairing, or replacing tissue, proteins are involved. Sometimes their role is to facilitate or to regulate; other
times it is to become part of a structure.

1. As Building Materials for growth and maintenance: From the moment of conception, proteins form the building blocks of muscles,
blood, and skin.

Examples:

a. To build a bone or a tooth, cells first lay down a matrix of the protein collagen and then fill it with crystals of calcium, phosphorus,
magnesium, fluoride, and other minerals.

b. Proteins are also needed for replacing dead or damaged cells. The life span of a skin cell is only about 30 days. As old skin cells are shed,
new cells made largely of protein grow from underneath to replace them.

3. Muscle cells make new proteins to grow larger and stronger in response to exercise.
 Roles of protein in the human body, Cont.

2. As Enzymes: Some proteins act as enzymes.

1. Digestive enzymes.

- Enzymes not only break down substances, but they also build
substances (such as bone) and transform one substance into another
(Such as amino acid into glucose).
 Roles of protein in the human body, Cont.
3. As Hormones: The body’s many hormones are messenger molecules, and some hormones are
proteins.

4. As Transporters: Some proteins move about in the body fluids, carrying nutrients and other
molecules.

- The protein hemoglobin carries oxygen from the lungs to the cells.

- The lipoproteins transport lipids around the body.

- Special transport proteins carry vitamins and minerals.

 Roles of protein in the human body, Cont.

5. As a Source of Energy and Glucose: Without energy, cells die; without glucose, the brain and nervous system falter. Even though
proteins are needed to do the work that only they can perform, they will be sacrificed to provide energy and glucose during times of
starvation or insufficient carbohydrate intake.

The body will break down its tissue proteins to make amino acids available for energy or glucose production. In this way, protein can
maintain blood glucose levels, but at the expense of losing lean body tissue.
 Part Three:
- Protein Quality
 Protein Quality
* The protein quality of the diet determines, in large part, how well children grow and how well adults maintain their health.

Meaning, high-quality proteins provide enough of all the essential amino acids needed to support the body’s work, and low-quality
proteins don’t.

Two factors influence protein quality: the protein’s digestibility and its amino acid composition.

1. Protein digestibility: depends on such factors as the protein’s source and the other foods eaten with it. The digestibility of most
animal proteins is high (90 to 99 percent); plant proteins are less digestible (70 to 90 percent for most, but more than 90 percent for soy
and legumes).

2. Amino Acid Composition To make proteins, a cell must have all the needed amino acids available simultaneously. The liver can make
any nonessential amino acid that may be in short supply so that the cells can continue linking amino acids into protein strands. If an
essential amino acid is missing, though, a cell must break its own proteins to obtain it.
 Protein Quality, Cont.

* High-Quality Proteins: A high-quality protein contains all the essential amino acids in relatively the same amounts and proportions
that human beings require; it may or may not contain all the nonessential amino acids.

* Proteins that are low in an essential amino acid cannot, by themselves, support protein synthesis.

- Generally, foods derived from animals (meat, fish, poultry, cheese, eggs, yogurt, and milk) provide high-quality proteins, although
gelatin is an exception. (It lacks tryptophan and cannot support growth and health as a diet’s sole protein.)

- Proteins from plants (vegetables, nuts, seeds, grains, and legumes) have more diverse amino acid patterns and tend to be limiting in one
or more essential amino acids. Some plant proteins are notoriously low quality (for example, corn protein). A few others are high quality
(for ex-ample, soy protein).
 Protein Quality, Cont.

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.
Part Four:
- Recommended intake of proteins

- Protein and amino acid supplements

 Recommended Intake of Protein

* Protein RDA: The protein RDA for adults is 0.8 grams per kilogram of healthy body weight per day. For infants and children, the
RDA is slightly higher.

- 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.

- The protein RDA is the same for athletes as for others, even though athletes may need more protein and many fitness authorities
recommend a higher range of protein intakes for athletes pursuing different activities

❖
 Protein & amino acid supplements
* Athletes take protein powders to build muscle. Dieters take them to spare their bodies’ protein while losing weight. Women take them to
strengthen their fingernails. People take individual amino acids to cure herpes, to make themselves sleep better, to lose weight, and to
relieve pain and depression.

* Whey protein: A product of cheese manufacturing. When combined with strength training, whey supplements may increase protein
synthesis slightly, but they do not seem to enhance athletic performance. To build stronger muscles, athletes need to eat food with adequate
energy and protein to support the weight-training work that does increase muscle mass.

* Branched chain AA: Advertisers point to research that identifies the BCAAs as the main ones used as fuel by exercising muscles, but they
leave out that these AA are very abundant in foods. Large doses of branched-chain amino acids can raise plasma ammonia concentrations,
which can be toxic to the brain, but can be helpful in patients with liver disease.