lecture #2date ______ chapter 4~ carbon & the molecular diversity of life chapter 5~ the...
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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
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You should know
• Atomic mass, atomic #, valence shells• Bonds
– Ionic– Covalent
• Polar (hydrophilic) vs Non-polar (hydrophobic)
– Hydrogen
• Isomer vs Isotope• Properties of H2O
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Practice
1) 7p, 7n, 7e
2) 7p, 8n, 7e
3) 8p, 7n, 7e
4) 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-?
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Organic chemistry
• Carbon-tetravalence-tetrahedron-shape
determines function
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Organic Compounds
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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)
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Testosterone vs Estrogen (fig. 4.8)
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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.
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Functional Groups – besides H
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Monomer vs Polymer
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Carbohydrates
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Monosaccharides – smallest unit
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Glucose Isomers
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Glycosidic Linkages
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Polysaccharides
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• 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
Uses of carbohydrates
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Simple vs Complex Carbs?
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Why are complex carbs better?
1. Weight management – take longer to eat
2. Fiber makes you feel fuller
3. Contain vitamins, minerals, etc.
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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)
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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
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Lipids – fats, waxes
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Triglycerides – contain C,
H, O(H:O > 2:1)
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Saturated vs Unsaturated
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Phospholipids - Amphipathic
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Steroids
• Lipids with 4 fused carbon rings
• Ex: cholesterol:cell membranes;precursor for other steroids (sex
hormones); atherosclerosis
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Are ALL Fats Bad?
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–Hydrogenating (adding hydrogen) unsaturated fats to make them solid (peanut butter and margarine) are just as unhealthy as saturated fats
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Unhydrogenated Peanut Butter
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• 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
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Good Things About Fat• More energy than carbs or
proteins• Helps absorb Vitamins A, C,
etc.• Healthy skin• Gives us fatty acids for growth
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The Good – Omega-3 Fats
• Lower blood pressure
• Decrease risk of heart attack
• Protect against irregular heartbeats
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How much should you eat?
YUM!
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• 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!
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NucleicAcid
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Proteins
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Amino Acids/Side Chains
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–Nonpolar – contain –CH2 or –CH3 (Hydrophobic)
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–Polar uncharged – Contain O or only –H (Hydrophilic)
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• Ionizable – acid (R groups are negative) or base groups (R groups = +)
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Peptide Bonds/Polypeptide
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Primary Structure – amino acid sequence
determines the protein
-If you switch 2 amino acids, you get a whole new
protein
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Amino acid substitution – 1 out of 600 amino acids
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Secondary Structure –
alpha helix & beta pleated
sheet
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Tertiary Structure
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Quaternary Structure – 2 or more polypeptides bond together
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Protein Folding Animation
• http://intro.bio.umb.edu/111-112/111F98Lect/folding.html
• http://intro.bio.umb.edu/111-112/111F98Lect/folding.html
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AP LAB 2
– Pre-Lab
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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?
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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)
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Homework
• Study for test
• Internet review – not for a grade
• No Quiz tomorrow – canceled– Quizzes – drop 1 per 9 weeks
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Protein Folding
Inactive Active
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Chemical Reactions/EA
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• Metabolism – all chemical reactions in a biological system
• Catabolism – breakdown of substances
• Anabolism – formation of new products
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Induced Fit
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Induced Fit
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Anabolic Enzyme
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Catabolic Enzyme
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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
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Enzyme Animations• http://highered.mcgraw-hill.com/sites/
0072495855/student_view0/chapter2/animation__how_enzymes_work.html
• http://highered.mcgraw-hill.com/sites/0072507470/student_view0/chapter25/animation__enzyme_action_and_the_hydrolysis_of_sucrose.html
• http://www.phschool.com/science/biology_place/labbench/lab2/binding.html
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Go over Quiz
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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
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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.
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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
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• 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
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• 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)
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Factors Affecting Enzyme Activity
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Cofactors/Coenzymes – other molecules that aid in enzymatic function (can bind along with the
enzyme)
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ATP/Energy Coupling
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Enzyme Regulation – Inhibition/Activation
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Allosteric Regulation
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Enzymes –Active and Allosteric
Sites
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Enzyme Animations
• http://www.northland.cc.mn.us/biology/biology1111/animations/enzyme.swf
• http://bcs.whfreeman.com/thelifewire/content/chp06/0602001.html
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Feedback Inhibition