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| 3318248011 | Properties of the combinations of Carbon and Hydrogen | -Nonpolar -Not soluble in H2O -Hydrophobic -Stable | 0 | |
| 3318249408 | Organic molecules | Molecules of life and are built around chains of carbon | 1 | |
| 3318250257 | Testosterone | Primary sex characteristics (male/female parts, sex drive, production of sperm) Secondary sex characteristics (more hair, more muscle tone) | 2 | |
| 3321592857 | Hydroxl | OH | 3 | |
| 3321593758 | Carbonyl | C=O | 4 | |
| 3321594816 | Carboxyl | COOH | 5 | |
| 3321596818 | Amine | NH2 | 6 | |
| 3321597867 | Sulfhydryl | SH | 7 | |
| 3321599346 | Phosphate | PO4 | 8 | |
| 3318253481 | Estradiol | Uterus lining thickness, egg formtation | 9 | |
| 3318254663 | Macro-molecules | Carbohydrates Lipids Protein Nucleic Acids | 10 | |
| 3318256043 | Polymer | Long molecules built by linking repeating building blocks in a chain | 11 | |
| 3318257199 | Monomers | Building blocks, repeated small units, covalent bonds | 12 | |
| 3318257959 | Condensation Reaction | Take out water in order to build a compound |  | 13 |
| 3318260145 | Anabolism | The synthesis of complex molecules from simpler molecules (joins monomers by taking h2o out, requires energy and enzymes) | 14 | |
| 3318262659 | Hydrolysis Reaction | Put in water in order to break down a compound into a single substance |  | 15 |
| 3318264720 | Catabolism | The breaking down of complex molecules into simpler molecules (requires enzymes, and releases energy) | 16 | |
| 3318267176 | Metabolism | The web of all the enzyme-catalyzed reactions in a cell or organism (catabolism+anabolism) | 17 | |
| 3318269947 | Carbohydrate Functions | Quick energy Energy storage Structure | 18 | |
| 3318272473 | Difference between aldehyde and ketone? | The positioning of the c=o | 19 | |
| 3318273326 | Monosacchrides | -Glucose -Galactose -Ribose -Fructose | 20 | |
| 3318274574 | Disaccharides | Maltose (glucose + glucose) Lactose (glucose + galactose) Sucrose (glucose + fructose) | 21 | |
| 3318281140 | Polysaccharides | Cellulose Starch Glycogen Chitin | 22 | |
| 3318283325 | Cellulose | -Unbranched beta-glucose -Linear -1,4 glycosidic linkage -Structural material in cell wall of plants -Rigid | 23 | |
| 3318287125 | Starch | Energy storage in plans a-glucos Amylose - Unbranched -1,4 glycosidic linkage -Slow release -Helix Amylopectin -Branched -1,4 and 1,6 glycosidic linkage -Helix | 24 | |
| 3318294157 | Glycogen | -alpha glucose -highly branched -helix 1,4 and 1,6 glycosidic linkage -quick release -storage in animals | 25 | |
| 3318297395 | Highly branched | More enzymes can attach to the molecule which means faster reaction | 26 | |
| 3318299741 | Lipids | -fats (nonpolar) -phospholipids -steroids | 27 | |
| 3318300440 | Lipid Function | -Long-term energy storage -Cushions organs -Insulates body | 28 | |
| 3318305509 | Saturated Fats | -All C bonded to H -Max number of hydrogens -No double bonds (C=O) -Straight and long -Solid at room temp |  | 29 |
| 3318310151 | Unsaturated fats | -Double bonds (C=O) -Liquid at room temp -Bent |  | 30 |
| 3318317517 | Phospholipid Structure | Glycerol + 2 fatty acids + PO4 (negative charge) -Makes the cell membrane |  | 31 |
| 3318320395 | Phospholipid hydrophobic or philic? | -Fatty acid tails = hydrophobic -PO4 head = hydrophilic -Makes the phospholipid bi-layer |  | 32 |
| 3318332688 | Building Fats | 3 fatty acids linked to glycerol with an ester linkage between OH and COOH |  | 33 |
| 3318338009 | Steroids | 4 fused C rings + (depends on what comes off the steroid) different functional groups to rings | 34 | |
| 3318340212 | Cholesterol | High level in blood may contribute to cardiovascular disease | 35 | |
| 3318342864 | What is cholesterol used for? | -Cell components -Animal cell membranes -Precursor of all other steroids | 36 | |
| 3318345099 | Protein Functions | Catalysis, cytoskeleton, tensile strengthening, blood clotting, transportation, cell adhesion, membrane transport, hormones, receptors, immunity, packing of DNA | 37 | |
| 3318351928 | Catalysis | A substance that increases the rate of reaction without altering anything else. It is not used up during the reaction, and can be used over and over again. | 38 | |
| 3318353147 | Cytoskeleton | a microscopic network of protein filaments and tubules in the cytoplasm of many living cells, giving them shape and coherence. | 39 | |
| 3318354323 | Tensile strengthening | Fibrous proteins. Strengthens ligaments, tendons, skin and blood vessel walls (collagen) | 40 | |
| 3318356426 | Blood clotting | Fibrin and Thrombin are used for blood clottin g | 41 | |
| 3318357864 | Transport | Hemoglobin transports O2 and CO2 | 42 | |
| 3318358686 | Cell adhesion | Proteins on the membrane cause cell to attach to each other within tissues | 43 | |
| 3318361171 | Membrane transport | Are used for active transport, electron transport, facilitated diffusion | 44 | |
| 3318363023 | Hormones | Chemical messengers that are manufactured by the endocrine glands, travel through the bloodstream, and affect other tissues (insulin) | 45 | |
| 3318371499 | Receptors | Special structures located on the membranes for hormones that allow living organisms to sense the conditions of their internal or external environment | 46 | |
| 3318374704 | Immunity | A condition of being able to resist a particular disease, especially through preventing development of a pathogenic microorganism or by counteracting the effects of its products. | 47 | |
| 3318376445 | Packing of DNA | During mitosis | 48 | |
| 3318378494 | Monomer of protein | Amino acid (20 diff amino acids) | 49 | |
| 3318380453 | Polymer of protein | Polypeptide (can be more than one polypeptide) | 50 | |
| 3318382841 | Amino acid structure | Central carbon, amino acid group, carboxyl (C=O), R group | 51 | |
| 3318384932 | What does the R group of an amino acid do? | It is different for each amino acid, and it confers unique chemical property and function | 52 | |
| 3318387113 | Nonpolar amino acids (hydrocarbon) | -Glycine -Alanine -Valine -Leucine |  | 53 |
| 3318388799 | Polar amino acids | -Serine (O2) -Theorine (O2) -Cysteine -Tyrosine (O2) -Asparagine (O2) | | 54 |
| 3318392739 | Sulfur containing amino acids | Form disulfide bridges (covalent cross links between sulfhydryls) |  | 55 |
| 3318398353 | Peptide bonds | Covalent bonds between NH2 of one amino acid and COOH of another amino acid |  | 56 |
| 3318401466 | Proteomes | All of the proteins produced by a cell, tissue, organism (what gene produced what protein) | 57 | |
| 3318406558 | Unfolding a protein (denaturing) | COnditions that disturb pH, Hydrogen bonds, Ionic bonds, and disulfide bridges | 58 | |
| 3318408657 | What denatures a protein | -Temperature -pH -Salinity | 59 | |
| 3318410907 | What does denaturing do? | Alters secondary and tertiary structure, and destroys functionality | 60 | |
| 3318413378 | Amino acid sequence | Amino acid sequence is coded for by the genes | 61 | |
| 3318414023 | Examples of protein | Rubisco, Insulin, Immoglobin, Rhodopsin, Collagen, Spider Silk | 62 | |
| 3318416624 | Rubisco | Captures CO2 in plants | 63 | |
| 3318418080 | Insulin | A protein hormone synthesized in the pancreas that regulates blood sugar levels by facilitating the uptake of glucose into tissues | 64 | |
| 3318418912 | Immoglobin | Antibodies, they bing/tag antigens that are foreign from pathogens (immune system) | 65 | |
| 3318420360 | Rhodopsin | Pigment found in the eye that absorbs light | 66 | |
| 3318421555 | Collagen | Fibrous protein that gives the skin form and strength | 67 | |
| 3318422992 | Spider Silk | structural protein that is used to make webs to catch preys. | 68 | |
| 3318445673 | Chemical reactions that release energy | Exergonic, digesting polymers, hydrolysis= catabolism | 69 | |
| 3318448326 | Chemical reactions that require energy | Endergonic, building polymers, condensation= anabolism | 70 | |
| 3318450275 | Exergonic reaction | Energy is released |  | 71 |
| 3318454544 | Endergonic reaciton | Energy is needed |  | 72 |
| 3318463681 | Activation Energy | Amount of energy needed to destabilize the bonds of a molecules (moves the reaction over an energy level) |  | 73 |
| 3318470868 | Reducing activation energy | Catalysts - Reducing the amount of energy to start a reaction make it react faster |  | 74 |
| 3318475250 | Enzymes | Increase rate of reaction without being consumed and reduce the activation energy without changing the free energy released or required | 75 | |
| 3318479115 | Substrate | Reactant which binds to enzyme | 76 | |
| 3318480656 | Product | End result of a reaction | 77 | |
| 3318481248 | Active site | Enzyme's catalytic site; substrate fits into active site |  | 78 |
| 3318488164 | Properties of enzymes | -Reaction specific -Not consumed in reaction -Affected by cellular conditions | 79 | |
| 3318490161 | Reaction specific (enzyme) | Each enzyme works with a specific substrate | 80 | |
| 3318490747 | Not consumed in reaction (enzymes) | Single enzyme molecules can catalyze thousands or more reactions per second | 81 | |
| 3318493356 | Affected by cellular conditions (enzymes) | Any condition that affects protein structure (temp, pH, salinity) | 82 | |
| 3318494847 | Naming conventions (enzymes) | Enzymes are named for reaction they catalyze (-ase) | 83 | |
| 3318496425 | Lock and Key Model | Simplistic model of enzyme action | 84 | |
| 3318497900 | Induced Fit Model | More accurate model of enzyme action, substrate binding cause enzyme to change shape in active site leading to a tighter fit | 85 | |
| 3318506317 | Synthesis (enzymes) | Active site orients substrate in correct position for reaction | 86 | |
| 3318507104 | Digestion (enzymes) | Active site bind substrate and puts stress on bonds that must be broken, making it easier to separate molecules | 87 | |
| 3318508792 | Factors that affect enzyme functions | Enzyme concentration, substrate concentration, temperature, pH, salinity, activators, inhibitors | 88 | |
| 3318524701 | Enzyme concentration (enzymes) | As enzyme increases, reaction rate increases, more enzyme =more frequently collide with substrate | 89 | |
| 3318528136 | Enzyme concentration reaction rate levels off | Substrate becomes limiting factor, not all enzymes molecules can find substrate |  | 90 |
| 3318529892 | Substrate concentration (enzymes) | As substrate increases, reaction rate increases, more substrate = more frequently collide with enzyme | 91 | |
| 3318532519 | Substrate concentration reaction rate levels off | all enzymes have active site engaged, all enzymes are saturated, max rate of reaction (only certain amount of active sites) |  | 92 |
| 3318535474 | Temperature (enzymes) | Depending on the temperature, the enzyme is going to denature or the molecules will move slower |  | 93 |
| 3318539009 | Optimum temp (enzymes) | Greatest number of molecular collisions (human enzymes = 35 C- 40 C) | 94 | |
| 3318542489 | Heat: increase beyond optimum temp (enzymes) | Denatures- increased energy level of molecules disrupts bonds in enzyme and between enzyme and substrate | 95 | |
| 3318548595 | Cold: decrease temp (enzymes) | Molecules move slower, decrease collisions between enzyme and substrate | 96 | |
| 3318550083 | pH (enzymes) | Depending on the level of pH the enzyme will denature or not | 97 | |
| 3318551926 | Changes in pH (enzymes) | adds or removes hydrogens, disturbs bonds between the amino acids, denature the protein | 98 | |
| 3318555170 | Optimal pH (enzymes) | Most humans = pH 6-8 Pepsin = pH 2-3 (stomach) Trypsin = pH 8 (small intestine) | 99 | |
| 3318557511 | Salinity (enzymes) | Changes in salinity will add or remove cations and anions and disrupt bonds | 100 | |
| 3318563624 | Activators (help) (enzymes) | Cofactors- nonprotein and small inorganic compounds and ions Coenzymes- nonprotein organic molecules that bind temporarily or perminatly to enzyme | 101 | |
| 3318568478 | Inhibitors (regulate enzymes) (enzymes) | Molecules that reduce enzyme activity -competitive inhibitions -noncompetitive inhibitions -irreversible inhibitions -feedback inhibitions | 102 | |
| 3318574554 | Competitive inhibitions (enzymes) | Inhibitor and substrate "compete" for active site (penicillin- blocks enzyme bacteria used to build cell walls) (disulfiram- treats chronic alcoholism) over come by increasing substrate concentration |  | 103 |
| 3318579839 | Noncompetitive inhibitions (enzymes) | Inhibitor binds to site other than active site |  | 104 |
| 3318586314 | Irreversible inhibition (enzymes) | Inhibitor permanently binds to enzyme | 105 | |
| 3318588061 | Irreversible inhibitions types (enzymes) | Competitor- permenently binds to active site Allosteric- permenantly binds to allosteric site and changes shape on enzyme | 106 | |
| 3320935349 | Allosteric Regulation | Conformational changes by regulatory molecule | 107 | |
| 3320937103 | Inhibitors (enzymes) | Keep enzyme in inactive form | 108 | |
| 3320937955 | Activators (enzymes) | keep enzyme in active form | 109 | |
| 3320943134 | Feedback Inhibition | Regulation and coordination of production |  | 110 |
| 3320949230 | Feedback inhibition procedure | Product is used by next step in pathway, final product in inhibitor of earlier step, not unnecessary accumulation of product | 111 | |
| 3320956280 | Metabolic Pathways | Chemical reactions of life are organized in pathways |  | 112 |
| 3320957931 | What metabolic pathways do? | Divide chemical reaction into many small steps | 113 | |
| 3320958700 | Lactose free milk | Sweeter than regular milk, monossaccharides are sweeter than dissaccharides and polymers, often times use lactose free milk to make ice cream because it has less ice crystals |  | 114 |
| 3320962827 | How lactase breaks down lactose | Lactase breaks down lactose into glucose and galactose, by pouring lactose into a container filled with lactase gelatin beads which then breaks it down. |  | 115 |
| 3321450050 | HONC? | Hydrogen, oxygen, nitrogen, carbon | 116 | |
| 3321453209 | Chemical re-activity | Atoms tend to complete/empty a partially fill valance shell | 117 | |
| 3321455291 | Hydrogen bonds | Weak bonds, attraction between (+) and (-) |  | 118 |
| 3321458381 | Hydrophobic and hydrophilic interactions | Interactions with H2O | 119 | |
| 3321459258 | Van derWaals forces | ionic | 120 | |
| 3321460196 | Covalent bonds | Atoms sharing electrons to make it strong and stable (forms molecules) |  | 121 |
| 3321462571 | Nonpolar covalent bonds | Pair of electrons shared equally by 2 atoms | 122 | |
| 3321463659 | Polar covalent bonds | Pair of electrons shared unequally by 2 atoms (water- oxygen has a stronger attraction for the electrons than hydrogen) | 123 | |
| 3321467501 | Hydrogen Bonding | Polar water creates molecular attractions, it is a weak bond | 124 | |
| 3321469019 | Chemistry of water | H2O molecules form hydrogen bonds with each other and create sticky molecules | 125 | |
| 3321470445 | Properties of water | Cohesion and adhesion, universal solvent, ice floats, high specific heat, heat of vaporization, | 126 | |
| 3321474362 | Cohesion | Water sticks to itself | 127 | |
| 3321475125 | Adhesion | Water sticks to other polar substances | 128 | |
| 3321476361 | Surface tension | Because of cohesion water sticks to itself which allows the surface tension to be hard to break | 129 | |
| 3321477936 | Capillary action | Because of cohesion and adhesion water is able to move up against gravity | 130 | |
| 3321480059 | Real world connection for adhesion and cohesion | When water moves up the roots of a plant through the xylem vessels to get to the leaves to make photosynthesis. | 131 | |
| 3321482129 | Universal solvent | Polarity makes water a good solvent which means solvents dissolve solutes creating solutions | 132 | |
| 3321484018 | Real world connection for universal solvent | Water transports nutrients in your body through your blood (glucose, amino acids, cholesterol, fats, oxygen, sodium chloride in blood) | 133 | |
| 3321485840 | Hydrophilic | Do attract to water (polar) | 134 | |
| 3321486453 | Hydrophobic | Don't attract to water (non-polar) | 135 | |
| 3321487620 | Ice floats | Water in solid form is less dense than water at liquid form (H bonds form a crystal) | 136 | |
| 3321490739 | Use for ice floats | Surface ice insulates water below allowing life to survive the winter | 137 | |
| 3321493790 | Use for ice floats #2 | If ice sank, it would kill all marine life and freeze solid | 138 | |
| 3321495432 | High specific heat | Water resists changes in temperature (takes a lot to heat it up and cool it down) | 139 | |
| 3321496252 | How does high specific heat work? | Energy absorbed when hydrogen bonds are broken | 140 | |
| 3321498508 | Real world connection for high specific heat | Moderates temperatures in the ocean and then that causes the moderation of temperature on Earth | 141 | |
| 3321500344 | Heat of vaporization | Cooling system allows people to sweat the heat off | 142 | |
| 3321502740 | Water vs Methane | water absorbs a lot of energy, while methane doesn't absorb a lot of energy | 143 | |
| 3321507057 | Water and pH | neutral = 7, acidic = 1-7, basic = 7-14 | 144 | |
| 3321508870 | Buffers | It reserves the amount of hydrogen, it can either add or subtract hydrogen from the solution to keep it at a regular pH | 145 | |
| 3321511181 | What is vitalism? | The belief that organic matter cannot be made by non organic matter | 146 | |
| 3321513300 | Who falsified it? | Wolher, by synthesizing urea (found in urine) | 147 | |
| 3321514675 | Paradigm shift | Idea change after prove it false | 148 | |
| 3321516804 | Draw a saturated fatty acid |  | 149 | |
| 3321517369 | Draw a unsaturated fatty acid |  | 150 | |
| 3321517393 | Draw an amino acid |  | 151 | |
| 3321518026 | Draw a D-ribose |  | 152 | |
| 3321519210 | Draw a-glucose |  | 153 | |
| 3321519652 | Draw b-glucose |  | 154 | |
| 3321524027 | B plated sheet |  | 155 | |
| 3321528663 | Molecular composition diagram for sugar |  | 156 | |
| 3321534891 | Molecular diagram for lipids |  | 157 | |
| 3321535876 | Trans and cis fatty acids | Unsaturated fatty acids can exist as trans and cis isomers | 158 | |
| 3321536735 | Trans fats | Not beneficial for human health, artificially made by pumping in hydrogen, packs together more tightly, increases risk of coronary heart disease | 159 | |
| 3321539563 | Hydrogen location on the trans fats | Hydrogen is located on the opposite side of the double bond producing a straight molecule | 160 | |
| 3321540884 | Cis fats | More natural than trans fats, pack less tightly | 161 | |
| 3321542632 | Hydrogen location on the cis fats | Have hydrogen on the same side of the double bond making the molecule bend | 162 | |
| 3321544938 | Molecular diagram for polypeptide |  | 163 |
