Proteins & Amino Acids - Chapter 6 Flashcards
Structure of the Basic Protein
- Composed of carbon, hydrogen, oxygen and nitrogen
- Arranged in strands of amino acids (AAs)
Basic Protein Structure & Function
- All AAs have the same chemical backbone
- A single carbon atom, with an amine group and an acid group attached
- Each AA has a distinctive side chain which gives it its identity and chemical nature
- The side chains make the AA differ in size, shape and electrical charge (positive, negative or neutral)
Basic Protein Structure
& Function (20 AAs)
- 8 indispensable/essential, some may become
conditionally essential (e.g., histidine) - Joined together by peptide bonds to form proteins
- 2 AA = dipeptide
- 3 AA = tripeptide
- > 3 AA = polypeptide
Building Protein
- AAs chemically attracted to or repelled from each
other- Creates a coil shape
- Spots along the coil attracted/repelled
- Globular structure or fibrous structure
Sequence & Shape Determine Function
- DNA (genetic sequence) determines the AA sequence in proteins
- Specific structure/shape of proteins enables them to perform different tasks in the body
Function of Protein
- Working proteins: enzymes, antibodies, hormones, oxygen carriers, etc.
- Structural proteins: tendons, ligaments, fibres of muscles, found in our bones, teeth, hair and nails
Protein Synthesis Errors
- For each protein, there exists a standard AA sequence which is specified by heredity
- If a wrong AA is inserted = health consequence
- E.g., genetic diseases
- Sickle cell disease
- E.g., genetic diseases
Protein Digestion (Stomach)
Gastric acid (HCl) denatures protein, and pepsin (enzyme) cleaves some
peptide bonds
Protein Digestion (Small intestine lumen)
Pancreatic enzymes cleave polypeptides to di- and tri-peptides
Protein Digestion (Brush border membrane)
Enzymes cleave di- and tri-peptides to single AAs
Protein Absorption
- Intestinal cells absorb AAs and some di- and tri peptides and release them into the bloodstream
- Absorbing larger peptides may contribute to food allergies (immune response)
- Carried to liver – used or released back into blood to be taken up by body cells
- Body can reconnect AAs to make proteins
- Body can use AA for energy if necessary
All Different Functions of Proteins (Part 1)
- Growth and maintenance
- Structure, new tissue, repair (e.g., RBC lifespan is 90-120 days)
- Hormones and enzymes
- E.g., growth factors, insulin
- Immune function
- Antibodies
All Different Functions of Proteins (Part 2)
- Fluid and electrolyte balance
- Protein transport
- E.g., protein malnutrition and edema
- Acid-base balance
- E.g., protein buffers
- Blood Clotting
- Energy (Fig. 6-12)- Secondary function,
only if diet is deficient
in carbohydrate or total energy - No storage form of
AAs
- Secondary function,
Protein Utilization (Build Protein)
- AA used to build proteins
- Converted to other small nitrogen-containing compounds, e.g.,
vitamins (tryptophan → niacin) - Converted to other AAs
- After removal of amino group:
- Gluconeogenesis: carbon skeleton → glucose → blood
- Lipogenesis: carbon skeleton → fat (for fuel or storage)
Protein Utilization (Waste)
- AAs are wasted when:
- Energy is lacking
- Protein is overabundant
- An AA is oversupplied (e.g., supplement)
- Diet has too few essential AA (i.e., low protein quality)
Protein Utilization (Protein Synthesis)
- To prevent wasting and permit protein synthesis:
- Dietary protein must be adequate and supply all essential AA in proper amounts
- Need adequate energy from carbohydrate and fat
Recommendations
- Recommendations for intake:
- DRI: 0.8g/kg body weight
- Females: 46g/day
- Males: 56g/day
- DRI minimum amount: 10% total energy
◦ DRI maximum amount: 35% total energy
- DRI: 0.8g/kg body weight
Protein Quality &
Quantity
- Malnutrition:
- Digestive enzyme secretion slows as the digestive tract lining degenerates, impairing protein digestion and absorption
- Infection:
- Protein is required to enhance immune function
- Efficient use of protein:
- Must be accompanied by the full array of vitamins and minerals