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Biochemistry and Honors Biology: Chemical Makeup of Living Things Explained

Learn about the 4 classes of compounds found in living things (carbohydrates, lipids, proteins, nucleic acids), their monomers and polymers, and the reactions involved in their formation. Understand the structure and function of biomolecules and their role in enzymes and hormones.

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Biochemistry and Honors Biology: Chemical Makeup of Living Things Explained

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  1. Biochemistry: the chemical makeup of living things A. General Information 1. There are 4 classes of compounds found in living things a. Carbohydrates – “sugars and starches” b. Lipids – “fats” c. Proteins – “enzymes, hormones,…” d. Nucleic acids – “DNA, RNA” 2. Carbon is the main element in all of the above classes a. needs 4 electrons to be stable (ie…can bond 4 times) b. forms covalent bonds Honors Biology: Chapter 3

  2. 3. Terms a. Monomer – simple molecule, that when repeated, builds a bigger molecule b. Polymer – the big molecule that is made from repeated monomers. c. Dehydration Reaction – name of the reaction when a polymer is made Monomer + Monomer + ……  Polymer + water d. Hydrolysis – name of the reaction when a polymer is broken into many monomers Water + Polymer  Monomer + Monomer + …

  3. Classes of Compounds A. Carbohydrates – “sugars and starches” 1. made of Carbon, hydrogen, and Oxygen 2. the monomer is a monosaccharide: examples: a. Glucose – plants make through photosynthesis b. Galactose – found in milk c. Fructose – found in fruit 3. all monosaccharides have the formula C6H12O6 4. they are “isomers” – they have the same formula, but different arrangement of atoms

  4. 5. Dissacharides: when 2 monosaccharides bond a. glucose + glucose  Maltose + water b. glucose + galactose  Lactose + water c. glucose + fructose  Sucrose + water 6. Polysaccharides: when many monosaccharides bond a. starch – how plants store extra glucose b. glycogen – how animals store extra glucose c. cellulose – found in cell walls of plants

  5. Glucose sucrose

  6. B. Lipids – “Fats, oils, waxes, and steroids” 1. made of Carbon, Hydrogen, and Oxygen 2. the monomer is a fatty acid a. drawing of a fatty acid: b. hydrophobic = water fearing (hydrocarbon end) c. hydrophilic = water loving (carboxyl group)

  7. 3. Saturated Fat – the hydrocarbon chain is saturated with hydrogens…therefore there are no double bonds in the chain a. can solidify because molecules can get close enough b. these are the “bad” ones c. drawing: 4. Unsaturated Fat – double bonds are in the hydrocarbon chain a. can’t solidify because the double bonds cause “kinks” b. drawing:

  8. Triglyceride Steroid -- Cholesterol

  9. C. Nucleic Acid 1. made of Carbon, Hydrogen, Oxygen, Nitrogen and Phosphorous 2. The monomer is a nucleotide 3. Polymers are DNA (holds the recipes to make protein) and RNA (helps to make the protein)

  10. D. Proteins 1. Made of Carbon, Hydrogen, Oxygen, and Nitrogen 2. The monomer is an amino acid 3. There are 20 amino acids that our bodies use to make all of our proteins 4. Types of proteins:

  11. Amino Acids

  12. Amino Acids

  13. 4. There are 4 levels of structure that go into determining the shape of a protein a. Primary Structure – amino acid sequence **This is what determines the 3D conformation b. Secondary Structure – coils and folds made by polypeptide chain **Coils caused by hydrogen bonds at regular intervals along the polypeptide chain **Alpha helix – coil held together by H-bonding between every 4th amino acid **Pleated sheet – two regions of the polypeptide chain lie parallel to each other

  14. c. Tertiary Structure – the overall, 3D shape of the polypeptide **most are described as “globular” or “fibrous” **results from the interactions between the R groups **Hydrophobic interaction – type of bonding that causes the tertiary structure **Disulfide bridges – strong covalent bonds that reinforce the protein conformation. Form when two cystein monomers are close together. d. Quaternary Structure – overall structure that results from the combination of more than one polypeptide folded chain. ** Not all proteins have this structure **Collagen and Hemoglobin are examples

  15. Primary Structure Secondary Structure Tertiary Structure Quaternary Structure

  16. 4. Enzymes – a type of protein that speeds up a reaction a. weakens chemical bonds to make them easier to break b. very specific to what molecule (substrate) it works on c. things can affect how well enzymes work (lab) **Concentration of enzyme **Temperature of environment **pH of environment **Enzyme inhibitors (poisons, antibiotics) Competitive inhibitors – block substrate from entering active site Allosteric inhibitors – bind to another part of the enzyme causing it to change shape and therefore unreceptive to the substrate Noncompetitive inhibitors – bind to another part of the enzyme causing it to change shape, but not so much that a reaction can’t take place. Reaction occurs, just slower. 5. Hormones – a type of protein that regulates body functions Toothpick Demo

  17. Enzyme Lab Info

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