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The Big Four. Are you what you eat?. 1. The important Characteristics of Carbon. Forms 4 covalent bonds Forms double and triple bonds Forms long chains and rings Can bind with many other elements Even electron distribution (nonpolar molecules).

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1 the important characteristics of carbon
1. The important Characteristics of Carbon
  • Forms 4 covalent bonds
  • Forms double and triple bonds
  • Forms long chains and rings
  • Can bind with many other elements
  • Even electron distribution (nonpolar molecules)






2 macromolecules monomers and polymers
2. Macromolecules, Monomers and Polymers
  • Polymer – Smaller organic molecules join into long chains.
  • Monomer – the individual unit that builds up polymers
  • Macromolecules – Very large molecules
3 dehydration synthesis and hydrolysis
3. Dehydration synthesis and Hydrolysis
  • These two terms refer to the processes that forms monomers and polymers:
    • Dehydration synthesis – A reaction that removes molecules of water to form polymers from monomers
    • Hydrolysis – The reaction that adds water to polymers to separate them to their individual monomers.
  • ( or )


    • Molecules that have the same formula, but different structures.
    • Examples: Glucose and Fructose
look at the label to the left 3 of the 4 macromolecules can be found in foods
Look at the label to the left. 3 of the 4 macromolecules can be found in foods.


  • 1____________________
  • 2____________________
  • 3____________________

(0 grams in this product)


(13 grams in this product)


(9 grams in this product)


What is the fourth

type of biochemical


4 what are the big four1
4. What are the big four?
  • Fats (we call them lipids)
  • Carbohydrates
  • Proteins
  • Nucleic acids (DNA and RNA)
when studying these biochemical molecules we are interested in finding out
When studying these biochemical molecules, we are interested in finding out…..
  • what they do for living things.
  • what they generally look like.
  • what their monomers are.
  • and how they may help the body gain energy to sustain life.


great website for reference
Great website for reference…
5 carbohydrates
5. Carbohydrates
  • Molecules that form from atoms in C1:H2:O1 ratio
  • Monomers: Monosaccharides (simple sugars)
  • Monosaccharides are usually sweet, white powdery substances (such as fructose, glucose) that form rings of carbon atoms.

Monosaccharides in general serve as direct, quick sources of energy for living organisms during cellular respiration, they are building blocks of many polymers

  • Important monosaccharides:
    • Glucose
    • Fructose

Disaccharides – two monosaccharide molecules combine by dehydration synthesis to form disaccharides


Important disaccharides:

    • Lactose – found in milk sugar
    • Sucrose – table sugar

Polysaccharides – many (tens to hundreds) units of monosaccharides combine by dehydration synthesis

  • Polysaccharides also separate to monosaccharides by hydrolysis while taking in water.

Important polysaccharides:

  • Starch – made up of many glucose units, it is an important storage polysaccharide that is found in plant roots and other tissues. It stores monosaccharides that can be broken down later to release useful energy during cellular respiration – ONLY IN PLANTS
  • Glycogen – also made up of many glucose units, it is an important storage polysaccharide in the liver and animal muscles. It can also be broken down to monomers to release energy during cellular respiration. ONLY IN ANIMALS
  • Cellulose – also made up of many glucose units. However, in this case the molecule is not easily broken down to its monomers. It is important for providing a rigid structure in plant cell walls.

Chitin – made up of some nitrogen containing monosaccharides. It is an important polysaccharide that provide the solid structure of arthropods and fungi.

6 lipids
6. Lipids
  • a diverse group of molecules that are nonpolar and generally do not dissolve in water
  • They mostly contain carbon, hydrogen, very few oxygen atoms, but some also have phosphorous.
  • There are three distinct groups of lipids:
    • Simple lipids
    • Phospholipids
    • Sterols
6a simple lipids
6A. Simple Lipids
  • Very large molecules that form from 2 different kinds of monomers by dehydration synthesis:
    • 3 Fatty acids – are long chains of carbon with oxygen at the end (can be saturated and unsaturated)
    • 1 Glycerol – smaller 3-carbon compound.

Simple lipids are important as storage materials in all living things. They can store twice as much energy as polysaccharides can.

  • Fatty tissue cushions vital organs and insulates the body.
  • Plant fats contain more unsaturated fatty acids, while animal fats contain more saturated fatty acids.
  • Simple lipids also dissolve vitamins
6b phospholipids
6B. Phospholipids
  • Phospholipids – phosphate containing lipids.
  • Their monomers: 1 glycerol + 2 fatty acids (saturated and unsaturated) + phosphate. These monomers combine by dehydration synthesis
  • Phospholipids have both polar and nonpolar sections. As a result, they are able to dissolve in both type of solvents as well.
  • They are important for living things because they form the borders of all cells (cell membranes) and also participate in forming many cell organelles.
6c sterols
  • Sterols are a highly nonpolar (hydrophobic) group of molecules.
  • They occur naturally in plants, animals, and fungi, with the most familiar type of animal sterol being cholesterol.
  • Cholesterol is vital to cellular function, and a precursor to fat-soluble vitamins and steroid hormones.
  • 3-six sided rings and one 5-sided ring + alcohol
7 proteins
7. Proteins
  • Protein- Polymer constructed from amino acid monomers.
  • Only 20 amino acids, but make 1,000s of proteins
  • Some are 100 a.a. in length; some are thousands

3-D Protein

7a protein functions
7A. Protein Functions
  • Each of our 1,000s of proteins has a unique 3-D shape that corresponds to a specific function:
    • Defensive proteins
      • Antibodies in your immune system
    • Signal proteins
      • Hormones and other messengers
    • Hemoglobin
      • Delivers 02 to working muscles
    • Transport proteins
      • Move sugar molecules into cells for energy (insulin)
    • Storage proteins
      • Ovalbumin (found in egg white) used as a source of amino acid for developing embryos
    • Most important roles is as enzymes
      • Chemical catalysts that speed and regulate virtually all chemical reactions in cells
      • Example, lactase
7b amino acid structure
7B. Amino Acid structure
  • Proteins diversity is based on differing arrangements of 20 amino acids.
  • Amino acids all have an amino group and a carboxyl group.
  • R group is the variable part of the amino acid; determine the specific properties of the 20 amino acids.
  • Two main types:
    • Hydrophobic
      • Example: Leucine
        • R group is nonpolar and hydrophobic
    • Hydrophilic
      • Polar and charged a.a.’s help proteins dissolve in aqueous solutions inside cells.
      • Example: Serine
        • R group is a hydroxl group
7c amino acid dehydration
7C. Amino Acid Dehydration
  • Cells join amino acids together in a dehydration reaction:
    • Links the carboxyl group of one amino acid to the amino group of the next amino acid as a water molecule is removed.
    • Form a covalent linkage called a peptide bond making a polypeptide.
7d protein structure
7D. Protein Structure
  • Primary Structure
    • Unique sequence of amino acids
    • For any protein to perform its specific function, it must have the correct collection of amino acids arranged in a precise order.
      • Example: a single amino acid change in hemoglobin causes sickle-cell disease
    • Determined by inherited genetic information.
7d protein structure1
7D. Protein Structure
  • Secondary Structure
    • Parts of the polypeptide coil or fold into local patterns.
      • Patterns are maintained by regularly spaced hydrogen bonds between the hydrogens of the amino group and the oxygen of the carboxyl groups.
    • Coiling results in an alpha helix.
      • Many fibrous proteins have the alpha structure over most of their length
      • Example: structural protein of hair
    • Folding leads to a pleated sheet.
      • Make up the core of many globular proteins
      • Dominate some fibrous proteins, including the silk proteins of a spider’s web
7d protein structure3
7D. Protein Structure
  • Tertiary Structure
    • Overall, three-dimensional shape of a polypeptide.
    • Roughly describe as either globular or fibrous
    • Generally results from interactions among the R groups of amino acids making up the polypeptide.
7d protein structure4
7D. Protein Structure
  • Quaternary Structure
    • Results from association of subunits between two or more polypeptide chains.
    • Does not form in every protein.
    • Example, Hemoglobin
8 nucleic acids
8. Nucleic Acids
  • Two types:
    • DNA and RNA
8 a dna
8 A. DNA
  • Deoxyribonucleic Acid (DNA)
    • Monomers made up of nucleotides:
      • Nucleotides consist of:
        • A five carbon sugar, deoxyribose
        • Phosphate group
        • Nitrogenous base (Adenine, Guanine, Cytosine, Thymine)
8a dna
  • As a Polymer, DNA is a…
  • Double helix consists of:
    • Sugar-phosphate backbone held by covalent bonds
    • Nitrogen bases are hydrogen bonded together; A pairs with T and C pairs with G
8a dna1
  • Consists of genetic material that organisms inherit from their parents.
  • Made up of genes:
    • Specific stretches of DNA that program amino acid sequences of proteins.
8b rna
  • Also made up of monomers of nucleotides
    • Nucleotide of RNA:
      • Sugar is ribose (not deoxyribose)
      • Phosphate group
      • Nitrogen bases (Adenine, Uracil (instead of Thymine, Guanine, and Cytosine)
8b rna1
  • Serves as a intermediary for making proteins
  • Consists of a single-strand
10 enzymes
10. Enzymes
  • Enzymes are proteins that act as biological catalysts in living organisms.
  • They speed up chemical reactions by lowering the activation energy of the reaction.

10a enzyme specificity
10A. Enzyme Specificity
  • Enzymes have a specific section called the active site that is able to bind with the reactants (substrates) of a chemical reaction
  • Once the substrates bind to the active site, the active site changes shape and pulls the reactants together. As a result, the reaction occurs faster and more efficiently.
  • The model that describes that enzymes change shape when bind with the substrate is called the induced fit model
10b induced fit model
10B. Induced Fit Model


10c enzyme characteristics
10C. Enzyme Characteristics
  • Three important special characteristics of enzymes:
    • They are specific
    • They are efficient
    • They are sensitive
10d cofactors and inhibitors
10D. Cofactors and Inhibitors
  • Cofactors:
    • Many enzyme do not function without an additional group attached to them. This additional group is called a cofactor.
  • Inhibitors:
    • Some substances can stop enzymes from functioning by attaching themselves to the active site of the enzyme. These are called inhibitors.
    • Many inhibitors are used as poisons or drugs.