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Lecture #2 Date ______ • Chapter 4~ Carbon & The Molecular Diversity of Life • Chapter 5~ The Structure & Function of Macromolecules • Objectives: – Chemistry Quiz – Compare and contrast the 4 groups of organic compounds You should know • Atomic mass, atomic #, valence shells • Bonds – Ionic – Covalent • Polar (hydrophilic) vs Non-polar (hydrophobic) – Hydrogen • Isomer vs Isotope • Properties of H2O Practice 1) 2) 3) 4) 7p, 7n, 7e 7p, 8n, 7e 8p, 7n, 7e 9p, 9n, 9e • How many different elements are here? • Which are the same? • Which has/have a charge of -1? • Which has/have an atomic weight of 15 amu? • Which has/have 1 valence e-? Organic chemistry • Carbon -tetravalence -tetrahedron -shape determines function Organic Compounds Hydrocarbons • Only carbon & hydrogen (petroleum; lipid ‘tails’) • Covalent bonding; nonpolar • High energy storage • Isomers (same molecular formula, but different structure & properties) – structural~differing covalent bonding arrangement – geometric~differing spatial arrangement – enantiomers~mirror images pharmacological industry (thalidomide – morning sickness drug) Testosterone vs Estrogen (fig. 4.8) Organic compounds • To build organic compounds you take hydrocarbon chains and add functional groups. • Molecules with the same functional groups will have similar physical and chemical properties. Functional Groups – besides H Monomer vs Polymer Carbohydrates Monosaccharides – smallest unit Glucose Isomers Glycosidic Linkages Polysaccharides Uses of carbohydrates • Polysaccharides – Storage: • Starch~ primary storage molecule for plants • Glycogen – storage molecule for animals (in liver and muscles), alpha links, can be broken down by human enzymes – Structural: • Cellulose~ most abundant organic compound; • Chitin~ exoskeletons; cell walls of fungi; surgical thread Simple vs Complex Carbs? Why are complex carbs better? 1. Weight management – take longer to eat 2. Fiber makes you feel fuller 3. Contain vitamins, minerals, etc. What happens when you eat too many carbs? • Excess carbs stored as fat • Simple carbs will cause a drastic increase in glucose – causes a release of insulin • Insulin then tells your body to store fat • Complex carbs do not cause a drastic increase in glucose levels (are broken down slowly) Low Carb Diets? • Carbs are needed to synthesize glycogen which are needed for effective workouts • Without glycogen, you cannot burn as much fat • Body uses fuel in this order (Glycogen, Fat, Muscle) • Low calorie diets can make your body burn muscle which causes a loss in total calorie burning potential – muscle cells have more mitochondria) • Weight comes off because of lost muscle but comes back as fat (NOT GOOD) • Ideal amount: 2000 cal diet = 250 g carbs Lipids – fats, waxes Triglycerides – contain C, H, O (H:O > 2:1) Saturated vs Unsaturated Phospholipids - Amphipathic Steroids • Lipids with 4 fused carbon rings • Ex: cholesterol: cell membranes; precursor for other steroids (sex hormones); atherosclerosis Are ALL Fats Bad? –Hydrogenating (adding hydrogen) unsaturated fats to make them solid (peanut butter and margarine) are just as unhealthy as saturated fats Unhydrogenated Peanut Butter • Men need 4-7% body fat • Women need 9-16% body fat • Going below these percentages is harmful since your body can’t perform all its normal functions Good Things About Fat • More energy than carbs or proteins • Helps absorb Vitamins A, C, etc. • Healthy skin • Gives us fatty acids for growth The Good – Omega-3 Fats • Lower blood pressure • Decrease risk of heart attack • Protect against irregular heartbeats How much should you eat? YUM! • You should consume 20 to 30% of your total calories from fat • No more than 10% should be saturated fats Too much or too little can be a health risk! Nucleic Acid Proteins Amino Acids/Side Chains –Nonpolar – contain –CH2 or –CH3 (Hydrophobic) –Polar uncharged – Contain O or only –H (Hydrophilic) • Ionizable – acid (R groups are negative) or base groups (R groups = +) Peptide Bonds/Polypeptide Primary Structure – amino acid sequence determines the protein -If you switch 2 amino acids, you get a whole new protein Amino acid substitution – 1 out of 600 amino acids Secondary Structure – alpha helix & beta pleated sheet Tertiary Structure Quaternary Structure – 2 or more polypeptides bond together Protein Folding Animation • http://intro.bio.umb.edu/111112/111F98Lect/folding.html • http://intro.bio.umb.edu/111112/111F98Lect/folding.html AP LAB 2 – Pre-Lab Warm-up - Have out your organic compounds WS – we will go over it 1. What bonding is associated with the following: – Primary structure of protein? – Secondary? – Tertiary? 2. What 2 main functions do proteins provide your body? 3. What four things does a amino acid have (structure)? 4. What is the smallest unit of a nucleic acid? What we’ve covered the last few days • Organic compounds – carb, lipid, protein, nucleic acid – Monomer, function, elements, examples – Able to recognize structural/molecular formulas • Enzymes – Protein folding – Characteristics – Environmental factors affecting rate (lab) – Regulation (end of class today) Homework • Study for test • Internet review – not for a grade • No Quiz tomorrow – canceled – Quizzes – drop 1 per 9 weeks Protein Folding Inactive Active Chemical Reactions/EA • Metabolism – all chemical reactions in a biological system • Catabolism – breakdown of substances • Anabolism – formation of new products Induced Fit Induced Fit Anabolic Enzyme Catabolic Enzyme Enzymes • • • • • Bind to substrate (molecule it acts on) Are specific (binds to certain substrate) Has active site (where substrate binds) Are reusable Are affected by temperature and pH Enzyme Animations • http://highered.mcgrawhill.com/sites/0072495855/student_view0/ chapter2/animation__how_enzymes_work. html • http://highered.mcgrawhill.com/sites/0072507470/student_view0/ chapter25/animation__enzyme_action_an d_the_hydrolysis_of_sucrose.html • http://www.phschool.com/science/biology_ place/labbench/lab2/binding.html Go over Quiz Finish Enzyme Lab • Safety Goggles – pH lab group, temperature group when heating • Whiteboard – data while you are finishing, be ready to explain data after lab Enzyme Lab Conclusion • Rate of reaction is determined by measuring the disappearance of substrate or the accumulation of product • Rate of reaction is the slope of the linear portion of the graph • Reaction rate is affected by pH, substrate conc., enzyme conc., temperature, and ionic con. Conclusions • Enzymes have optimum pH, temperature, and salt concentrations that they work in • General rules – Temp • Lower the temp, the slower the molecules collide – slower the reaction rate • Higher the temp, the faster the molecules move around – faster the reaction rate • Too high a temperature (60-70 C) – protein denatures – reaction doesn’t occur • pH – too high or too low the H+ or OH – ions react with the amino acid side chains (R groups) – improper folding occurs – reaction slows • Salt conc. – too much or too little causes improper folding of protein • Substrate concentration – lower the substrate conc., the slower the reaction • 6. After an enzyme is mixed with its substrate, the amount of product formed is determined at 10-second intervals for 1 minute. Data from this experiment are shown below: Time (sec) 0 10 20 30 40 50 60 Product formed (mg) 0.00 0.25 0.50 0.70 0.80 0.85 0.85 • What is the initial rate of this enzymatic reaction? Show your calculation. .025 mg/sec • What is the rate after 50 seconds? Show your calculation. Why is it different from the initial rate? .02125/sec (substrate is running out) Factors Affecting Enzyme Activity Cofactors/Coenzymes – other molecules that aid in enzymatic function (can bind along with the enzyme) ATP/Energy Coupling Enzyme Regulation – Inhibition/Activation Allosteric Regulation Enzymes – Active and Allosteric Sites Enzyme Animations • http://www.northland.cc.mn.us/biology/biol ogy1111/animations/enzyme.swf • http://bcs.whfreeman.com/thelifewire/conte nt/chp06/0602001.html Feedback Inhibition