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Name: Biomolecules Test Review -KEY 1. What are the 4 large categories of organic compounds that we call biomolecules? Proteins Carbohydrates Lipids Nucleic Acids 2. What are examples of each biomolecule? Examples Starch, glucose, Cellulose, Glycogen Biomolecule (polymer) Carbohydrate Oils, waxes, fats, vitamins, steroids, cell membranes DNA, RNA, ATP Lipids Enzymes, Insulin, Antibodies, Hemoglobin Proteins Nucleic Acids 3. How are monomers and polymers related? Polymers are long chains of single units called Monomers. 4. What is the difference in dehydration synthesis and hydrolysis? Use monomer(s) and polymer(s) in your explanation. In which process is water used? Released? – Dehydration Synthesis During dehydration synthesis monomers are linked together by the removal of a water molecule producing a polymer; which is the opposite of what occurs during hydrolysis. Hydrolysis adds water to a polymer, breaking the bonds holding the polymer together, resulting in individual monomers. 5. What are the monomers for each biomolecule? Monomer Monosaccharide Biomolecule (polymer) Carbohydrates Fatty Acids Lipids Nucleotides Nucleic Acids Amino Acids Protein 6. What elements make up each type of biomolecule? (use the element’s symbol) Elements CHO Biomolecule (polymer) Carbohydrates CHO Lipids CHONP Nucleic Acids C H O N sometimes S Protein Name: 7. How do you know C6H12O6 is a carbohydrate and not a lipid, protein, or nucleic acid? Because the Hydrogen and Oxygen are in a 2:1 ratio and there is no N or P 8. Glucose, one type of monosaccharide, is represented by the chemical formula, C6H12O6. If you were to put together 2 glucose molecules, why wouldn’t the molecular formula for the newly made disaccharide be C12H24O12? In order to link the 2 molecules together a water molecule must be removed (dehydration synthesis) the resulting formula would be: C6H12O6 + C6H12O6 C12H22O11 + H2O 9. What is the difference between saturated and unsaturated fatty acid? Which is better for you? Why? Saturated fatty acid- single bonds, straight and tightly packed. Solid at room temperature. (Bad for us!) Unsaturated fatty acid- double bonds bend the tails and it’s crooked (not straight). Liquid at room temperature (ex. Olive Oil) 10. For proteins to function (work) they have to be folded in several conformations A. B. C. D. Primary – sequence of amino acids Secondary – coiled into a helix or pleat Tertiary – folded into a “glob” that has an active site – it works in this shape Quaternary – 2 or more tertiaries (globs) that are held together by a metal ion (i.e iron holds hemoglobin together; copper holds myoglobin together) What (molecule) directs or determines their primary conformation? DNA 11. When a protein is denatured, what does that mean? What can denature a protein (name 2)? Denatured means that it changes shape and would no longer function properly. Temperature and pH are 2 things that can denature a protein. 12. Nucleotides are the monomers of nucleic acids like DNA and RNA. What 3 things make up a nucleotide? 1. 5-carbon sugar (pentose) 2. Phosphate group 3. Nitrogenous Base 13. Which nitrogenous base pairs bond together in deoxyribonucleic acid? Ribonucleic acid? How do they differ? Base Pairs DNA A–T C-G RNA A –U C-G Name: 14. What are enzymes? How do they function? Enzymes are a catalyst. Catalysts are used to speed up a reaction by decreasing the amount of energy needed to get the reaction started…Lowers the activation energy. 15. What factors affect the rate at which enzymes function? Explain how each would affect the enzymes rate of reaction. Factors that Affect Rate at Which Enzymes Function Temperature How would it affect rate of reaction? To hot or cold reaction would be inhibited pH pH to acidic or basic for that enzyme would inhibit reaction More enzymes the faster the substrate is acted upon Higher concentration would slow down total reaction speed Enzyme Concentration Substrate Concentration 16. Using the diagrams shown: IDENTIFY and LABEL the active site, substrate, enzyme and product. Substrate Active Site Products Enzyme Using the illustration above to describe what happens at each step: Step 1: Substrate attaches to the enzyme at the active site (Like a lock and key it must be the right shape in order to fit…doesn’t fit doesn’t work) Step 2: Enzyme substrate complex formed – Reaction occurs Step 3 (What happens to the enzyme?): Products are released from the enzyme. Enzyme remains unchanged and is available to do the reaction again if more substrate is available. 17. Compare competitive and noncompetitive inhibition and how it affects enzyme function. A noncompetitive inhibitor - is a substance that interacts with the enzyme, but usually not at the active site. The noncompetitive inhibitor reacts either remote from or very close to the active site. The net effect of a noncompetitive inhibitor is to change the shape of the enzyme and thus the active site, so that the substrate can no longer interact with the enzyme to give a reaction. Non-competitive inhibitors are usually reversible, but are not influenced by concentrations of the substrate as is the case for a reversible competitive inhibitor. A competitive inhibitor - is any compound which closely resembles the chemical structure and molecular Name: geometry of the substrate. The inhibitor competes for the same active site as the substrate molecule. The inhibitor may interact with the enzyme at the active site, but no reaction takes place. The inhibitor is "stuck" on the enzyme and prevents any substrate molecules from reacting with the enzyme. However, a competitive inhibition is usually reversible if sufficient substrate molecules are available to ultimately displace the inhibitor. Therefore, the amount of enzyme inhibition depends upon the inhibitor concentration, substrate concentration, and the relative affinities of the inhibitor and substrate for the active site. Name: 18. Complete the following chart: Protein Nucleic Acids Carbohydrates Lipids Elements in biomolecule C, H, O, & N Sometimes S C, H, O, N, & P C, H, O Hydrogen and Oxygen (2:1) C, H, O Hydrogen and Oxygen (greater than 2:1) Where synthesized in the cell Function(s) of biomolecule Ribosome Nucleus Chloroplast Smooth ER Catalyst, Maintenance, Repair, growth, transport, and metabolism Genetic Code Blueprints of DNA Cellular Energy Short term energy storage Structural support Primary fuel source Monomer Amino Acids Nucleotides Examples Meat, cheese, Milk Insulin, Hemoglobin, Antibodies, and Enzymes RNA, DNA, & ATP Monosaccharides (simple sugars) Potatoes, Rice, sugars (glucose, sucrose, lactose, & Fructose) Cellulose, and Chitin Long term energy storage Cushion Insulation Vitamins Steroids Plasma Membranes Fatty Acids Fats, Oils, Waxes, Steroids, & Vitamins 19. Where are the following digestive enzymes found and what are their roles in digestion? Enzyme Trypsin Amylase Pepsin Lipase Location Small Intestine Mouth/ Small Intestine Stomach Small Intestine Role Continues to break down Proteins Breakdown simple sugars Breaks down proteins into large peptides Breaks down Lipids Name: 20. Identify each of the following molecules Carbohydrate Nucleic Acid (ATP) Lipid (Triglyceride) Carbohydrate Lipid (Saturated Fat) Carbohydrate Protein Lipid (Unsaturated Fat) Protein Protein Carbohydrate Nucleic Acid Lipid (phospholipid)