Protein

Cards (72)

  • elemental composition
    carbon hydrogen oxygen nitrogen
  • Amino acid structure

    • Contains an amino group (NH2), a carboxyl group (COOH), a central carbon (C), and a variable group (R) that changes with each amino acid
  • Amino acids

    • When the variable group (R) is hydrogen (H) the amino acid is glycine
    • When the variable group (R) is HS-CH₂ the amino acid is cysteine
  • Elements found in proteins
    • Carbon (C)
    • Hydrogen (H)
    • Oxygen (O)
    • Nitrogen (N)
    • Sulfur (S)
    • Iron (Fe)
    • Phosphorus (P)
  • Essential amino acids

    Cannot be manufactured by the body, therefore must be obtained from food
  • Essential amino acids

    • Valine
    • Lysine
    • Leucine
    • Isoleucine
    • Phenylalanine
    • Methionine
    • Threonine
    • Tryptophan
    • Histidine (children)
    • Arginine (children)
  • Non-essential amino acids

    Can be manufactured by the body, therefore do not need to be obtained from food
  • Non-essential amino acids

    • Alanine
    • Aspartic acid
    • Cysteine
    • Ornithine
    • Serine
    • Asparagine
    • Proline
    • Tyrosine
    • Glycine
    • Glutamic acid
  • Proteins are one of the macronutrients. Proteins form the main part of all cells and tissues, making them essential for growth and repair.
  • Proteins are large molecules composed of amino acids. Amino acids are joined together by peptide links to form long polypeptide chains that make up proteins.
  • The human body uses 20 different amino acids to make all the proteins it needs to function. These are all found in food.
  • Peptide links

    Formed when two amino acids join together, resulting in the loss of a water (H2O) molecule in a condensation reaction
  • Stages in the formation of peptide links

    1. The COOH (acidic) group of one amino acid reacts with the NH₂ (basic) group of another
    2. The COOH (acidic) group loses an OH group, the NH₂ (basic) group loses a hydrogen (H) atom, and a water (H₂O) molecule is lost
    3. The result is a CO-NH bond, forming a dipeptide (two amino acids joined together)
  • When more than 20 amino acids join together, a polypeptide is formed. When more than 50 amino acids join together, a protein is formed. Each protein consists of one or more polypeptide chains.
  • Hydrolysis
    The reverse of the condensation reaction, involving the addition of water and enzyme action, occurring during digestion when proteins are broken down into individual amino acids
  • Primary structure of proteins

    • The order or sequence of amino acids in protein chains.
    • insulin is one of the simplest proteins containing 51 amino acids
  • Secondary structure of proteins

    • The folding of the primary structure of proteins into definite shapes, with polypeptide chains either folding in on themselves or cross-linking with another polypeptide chain
  • Disulfide bonds

    • Formed when two sulfurs from two amino acids (cysteine) join together from either a single polypeptide chain or two different polypeptide chains
  • Hydrogen bonds

    • Formed when a hydrogen (H) from the N-H group of one amino acid and an oxygen (O) from the C=O group of another amino acid join together from either a single polypeptide chain or two different polypeptide chains
  • Tertiary structure

    • Involves the folding of the secondary structure of proteins into three-dimensional shapes
    • Further cross-linking between amino acids forms definite shapes, which may be fibrous (elongated) or globular (folded over itself to form a compressed unit)
  • Fibrous
    Polypeptide chains are arranged in straight, spiral or zigzag shapes
  • Globular
    Polypeptide chains are arranged in a globular shape
  • Fibrous protein shapes

    • Straight
    • Spiral
    • Zigzag
  • Fibrous proteins

    • Insoluble in water
    • Not easily denatured
  • Globular proteins

    • Soluble in water
    • Easily denatured
  • Fibrous proteins

    • Gluten (wheat)
    • Elastin and collagen (meat connective tissue)
  • Globular proteins

    • Ovalbumin (egg white)
    • Lactalbumin (milk)
  • Conjugated proteins

    Proteins that combine with a non-protein molecule
  • Conjugated proteins

    • Lipoproteins (lipid and protein)
    • Phosphoproteins (phosphate and protein)
  • Conjugated protein examples

    • Lecithin
    • Caseinogen
  • Animal protein sources

    • Meat
    • Fish
    • Eggs
    • Milk
    • Cheese
  • Plant protein sources

    • Beans
    • Nuts
    • Lentils
    • Peas
    • Cereals
  • Biological value
    A measure of the protein quality in a food, displayed as a percentage. It is determined by the number of essential amino acids a food contains in proportion to the needs of the body.
  • High biological value (HBV) proteins

    Contain all essential amino acids, mostly found in animal sources with the exception of soya beans
  • Low biological value (LBV) proteins

    Lack one or more of the essential amino acids, mostly found in plant sources with the exception of gelatine
  • LBV protein sources

    • Wheat
    • Maize
    • Meat bones
  • Simple protein groups

    • Animal fibrous
    • Animal globular
    • Plant
  • Animal fibrous proteins

    • Elastin
    • Collagen
  • Animal globular proteins

    • Ovalbumin
    • Lactalbumin
  • Plant proteins

    • Glutenins- Glutenin, oryzenin

    • Prolamines- gliadin, zein