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| 5261603984 | __, __, __, __ make up 96% of living things | C H O N | 0 | |
| 5261615790 | __, __, __, __ most of the remaining 4% | P S Ca K | 1 | |
| 5261620917 | Trace Elements | Required; minute amounts Fe, I | 2 | |
| 5261632791 | Atomic Number | # of protons # of electrons in a stable atom of an element | 3 | |
| 5261642303 | Atomic Mass | Sum of protons and neutrons Electron mass is small and almost negligible | 4 | |
| 5261658599 | Atoms bond in order to fill... | valence shell | 5 | |
| 5261660911 | Octet Rule | Most atoms "want" 8 valence electrons and will share, steal, or give away electrons in order to fill valence shells | 6 | |
| 5261673482 | Octet Rule Exceptions | those w/ <6 total electrons | 7 | |
| 5261680550 | Covalent Bonding | Valence electrons shared Form molecules Single, double, triple bonds possible | 8 | |
| 5261690226 | Nonpolar Covalent | Electrons are shared equally O2 | 9 | |
| 5261692535 | Polar Covalent | Electrons are not shared equally The more electronegative atom exerts a greater pull on the electrons being shared H2O | 10 | |
| 5261711256 | In biology ___ bonds are considered stronger | Covalent | 11 | |
| 5261717455 | Ionic Bonding | Electrons are lost or gained from the outer shell in order to fulfill the octet rule Water can dissociate ionic bonds easily | 12 | |
| 5261734884 | Hydrogen Bonding | Weak bonds formed between molecules that contain polar covalent bonds | 13 | |
| 5261741346 | Molecular Structure vs Function | Each molecule has a characteristic size and shape which determine its function | 14 | |
| 5261759793 | Cohesion | Sticks together | 15 | |
| 5261759794 | Adhesion | Sticks to other things | 16 | |
| 5261759851 | High surface tension | water feels solid when you hit it bonds tighten | 17 | |
| 5261765401 | High specific heat | Amt of heat absorbed or lost to change 1g of substance by 1 degree C REsists temp change Keeps earth w/in viable temp limits | 18 | |
| 5261799034 | Water also has ____ & _____ | High heat of vaporization, evaporative cooling | 19 | |
| 5261807001 | Density of ice | less dense than liquid H bonds freeze and force molecules further apart in large bodies of water, top layer of ice insulates water below | 20 | |
| 5261819771 | Water is most dense at | 4 degrees C | 21 | |
| 5261831399 | Universal solvent | dissolves materials creating aqueous solutions | 22 | |
| 5261842253 | Water= ____ What's being dissolved = _____ | Solvent, solute | 23 | |
| 5261849952 | Direct result of water's polarity | Hydrophilic Hydrophobic | 24 | |
| 5261856713 | Water pH | Pure water (H+) concentration (OH-) Adding acids or bases changes concentrations quickly | 25 | |
| 5261872792 | pH is the measure of ____. | hydrogen ion concentration 0-14 | 26 | |
| 5261876190 | Acids | Donate H+ ions The more acidic a solution higher H+ concentration taste: sour | 27 | |
| 5261884716 | Bases | Some donate OH- ions Basic solution: lower H+ concentration, higher pH value taste: bitter | 28 | |
| 5261898503 | Buffer | Resist changes in pH Many in body (even minor changes can be life threatening) Blood: 7.4 | 29 | |
| 5261913524 | Hydrocarbons | Combinations of C & H Nonpolar not soluble in H20 hydrophobic stable little attraction between molecules gas at room temp | 30 | |
| 5261929280 | Isomers | Molecules with some molecular formula but different structure | 31 | |
| 5261938537 | Isomers have different ____ & ______. | Chemical properties, Biological functions | 32 | |
| 5261950371 | Organic compounds | contains carbon chains divided into 4 families | 33 | |
| 5261965825 | Functional Groups | Parts of organic compounds most commonly involved in chemical reactions Determine what bonds will be formed and functions of specific compounds | 34 | |
| 5261978386 | Hydroxyl | -OH Organic compounds with OH- alcohols Names typically end in -ol ex. ethanol |  | 35 |
| 5262009560 | Carbonyl | C=O Aldehyde and Ketone | 36 | |
| 5262018743 | Aldehyde | end of molecule (double bond) |  | 37 |
| 5262018744 | Ketone | middle of molecule |  | 38 |
| 5262037551 | Carboxyl | -COOH compounds with this: acids ex. fatty and amino acids |  | 39 |
| 5262043142 | Amino | -NH2 compounds with this: amines ex. amino acids acts as a base ammonia picks up H+ from solution |  | 40 |
| 5262059574 | Sulfhydryl | -SH Stabilize the structure of proteins |  | 41 |
| 5262067421 | Phosphate | -PO4 Increases gene expression lots of O= lots of negative charge highly reactive transfers energy between organic molecules |  | 42 |
| 5262092282 | Carbohydrates | Provide energy ex. candy, sugar, pasta, bread | 43 | |
| 5262099077 | Carbohydrates contain ___ & ___ | hydroxyl and carbonyl | 44 | |
| 5262104990 | Three groups of carbohydrates | Monosaccharides Disaccharides Polysaccharides | 45 | |
| 5262113926 | _____ are the bodies first choice of energy | carbohydrates constant surplus, everything else will be stored up (cause weight gain) | 46 | |
| 5262122422 | Monosaccharides | Carb monomer ex. glucose and fructose Formula CH2O | 47 | |
| 5262134358 | Disaccharides | Double sugars ex. sucrose, lactose, maltose formed by dehydration synthesis | 48 | |
| 5262148589 | Glycosidic linkage | bond formed between monosaccharides | 49 | |
| 5262153676 | Dehydration synthesis | Monosaccharide + monosaccharide -> disaccharide + water | 50 | |
| 5261759727 | Methyl | CH3 | 51 | |
| 5268822979 | Carbon forms ___ | 4 bonds | 52 | |
| 5268825873 | Hydrogen forms ___ | 1 bond | 53 | |
| 5268828635 | Oxygen forms ____ | 2 bonds | 54 | |
| 5268831364 | Nitrogen forms ____ | 3 bonds | 55 | |
| 5268854430 | Polysaccharides | complex | 56 | |
| 5268856941 | Polysaccharide examples | starch, cellulose, glycogen | 57 | |
| 5268865358 | Polysaccharides are ___ & _____ ______ for energy | stored and broken down | 58 | |
| 5268875726 | What is added to break polysaccharides apart? | Water | 59 | |
| 5268879824 | Polysaccharide: Cellulose | Most abundant organic compound on earth Indigestible roughage | 60 | |
| 5268894413 | Herbivores evolved mechanism to digest ___. Most carnivores have not | cellulose | 61 | |
| 5268901131 | Indicators of Carbohydrates | Benedict's solution Iodine | 62 | |
| 5268906819 | Benedict's | Blue to orange in monosaccharide | 63 | |
| 5268908939 | Iodine | amber to black in polysaccharide | 64 | |
| 5268917733 | Lipids | hydrophobic smaller than true polymers varied in form and function | 65 | |
| 5268930568 | Types of lipids | fats, phospholipids, steroids, waxes and oils | 66 | |
| 5268934681 | Lipid Monomer | Fatty Acids and Glycerol | 67 | |
| 5268937436 | Fats: monomers examples | glycerol, fatty acids | 68 | |
| 5268945476 | Ester linkage | bond between fatty acids and glycerol formed by dehydration synthesis | 69 | |
| 5268961253 | Fats function in energy _____ & _____. | storage and protection | 70 | |
| 5268967423 | Saturated | solid @ room temp | 71 | |
| 5272242271 | Saturated fats examples | butter, coconut oil, animal fats | 72 | |
| 5272275119 | Saturated fats bonds | No double bonds between carbons | 73 | |
| 5272278760 | Unsaturated | Liquid @ room temp | 74 | |
| 5272282893 | Unsaturated ex. | Plant oils | 75 | |
| 5272286291 | Unsaturated fats bonds | Double bonds between carbons (do not have max # of hydrogens) | 76 | |
| 5272295983 | Phospholipids | Similar to fats but w/ 2 fatty acids rather than 3 | 77 | |
| 5272303686 | Phospholipids OH group | 3rd -OH group of glycerol joined to -PO4 group | 78 | |
| 5272313216 | Phospholipids and water | Ambivalent behavior toward water (likes and dislikes) | 79 | |
| 5272318679 | Phospholipid tails | hydrophobic | 80 | |
| 5272328095 | Phosphate heads | neg charge and hydrophilic | 81 | |
| 5272330053 | Phospholipids component | major component of cellular membranes | 82 | |
| 5272340223 | Steroids | carbon skeleton of 4 fused rings | 83 | |
| 5272343600 | Steroid use | animal cell membranes and hormones | 84 | |
| 5272364802 | Protein monomers | amino acids | 85 | |
| 5272381352 | Proteins contain | amino and carboxyl groups | 86 | |
| 5272385276 | Protein use | support storage transport signaling immunity metabolism | 87 | |
| 5272391383 | Protein structure | sophisticated in structure and function | 88 | |
| 5272395735 | Protein accounts for | more than 50% of dry weight | 89 | |
| 5272406078 | Amino Acid groups | amino, carboxyl, R-group | 90 | |
| 5272413782 | Amino acid R-group | variable groups different for each amino acid | 91 | |
| 5272422131 | R-group properties | unique chemical properties to each amino acid | 92 | |
| 5272434321 | Peptides | Individual amino acids or Sequence of 2+ aminos created by dehydration synthesis | 93 | |
| 5272442546 | Peptide bond | between amino acids | 94 | |
| 5272451161 | Primary protein structure | Unique sequence; has to be exact sequences | 95 | |
| 5272451162 | Primary protein example | hemoglobin normal vs sickled insulin | 96 | |
| 5272454683 | Secondary protein structure | initial coiling and folding patterns that result from hydrogen bonds | 97 | |
| 5272454684 | Secondary protein example | alpha helix - coils pleated sheet - folds | 98 | |
| 5272459550 | Tertiary protein structure | Secondary coiling and folding | 99 | |
| 5272463104 | Quaternary protein structure | Overall protein structure that comes from the way all the polypeptide subunits are situated | 100 | |
| 5272508232 | Structure of proteins affected by | pH salt concentration temp other environmental factors | 101 | |
| 5272520146 | When protein structure changes | function changes (denatured= inactive) | 102 | |
| 5272529195 | Protein denaturation | Unfolding a protein, destroys functionality | 103 | |
| 5272536107 | Denaturing conditions | disrupt H bonds, ionic bonds, disulfide bridges | 104 | |
| 5272549708 | Sickle cell anemia | folds are different longer spread out protein hydrophobic | 105 | |
| 5272556306 | Biurets | indicator of protein blue -> violet in protein | 106 | |
| 5272565633 | Nucleic Acids | Store and transmit hereditary information | 107 | |
| 5272567625 | Nucleic Acid ex | DNA, RNA | 108 | |
| 5272574840 | Phosphodiester bond | bond between nucleotides | 109 | |
| 5272577604 | Nucleotides contain | sugar, phosphate group, nitrogen base (A,T,C,G) | 110 | |
| 5272592029 | Eat to make more | DNA, RNA | 111 | |
| 5272618288 | Metabolism | total amount of organism's chemical processes and reactions | 112 | |
| 5272621129 | catabolic | breakdowns (molecules) release energy | 113 | |
| 5272625618 | catabolic ex | cellular respiration where glucose is broken down and ATP is released, digestion | 114 | |
| 5272631607 | anabolic | reactions that build complex molecules from simpler ones requires energy input | 115 | |
| 5272634049 | anabolic ex | synthesis of proteins from amino acids | 116 | |
| 5272644792 | 1st law of thermodynamics | Energy can be transferred and transformed, but neither created nor destroyed | 117 | |
| 5272653332 | 2nd law of thermodynamics | Every energy transfer makes universe more disordered (entropy) | 118 | |
| 5272658931 | 2nd law example | heat is energy in its most random state | 119 | |
| 5272664637 | Free energy | available for work represented: G | 120 | |
| 5272677112 | Exergonic | Release free energy catabolic | 121 | |
| 5272680050 | Exergonic ex | cellular respiration | 122 | |
| 5272682527 | Endergonic | absorbs free energy anabolic | 123 | |
| 5272686598 | Endergonic ex | photosynthesis (input of solar energy) | 124 | |
| 5272693512 | Mechanical cellular work | movement ex. muscle contractions | 125 | |
| 5272695971 | Transport cellular work | pumping of substances across membranes | 126 | |
| 5272695972 | Chemical cellular work | pushing of endergonic reactions that do not occur spontaneously ex. dehydration synthesis | 127 | |
| 5272711518 | ATP | Energy molecule used to power cellular work | 128 | |
| 5272724580 | Cause of release of free energy | hydrolysis of last phosphate group | 129 | |
| 5272731014 | Renewable molecule ATP | regenerated by addition of phosphate group of ATP | 130 | |
| 5272736876 | ATP contains | 3 phosphate groups @ end | 131 | |
| 5272742945 | Competitive inhibition | another molecule competes directly for enzyme active site and blocks substrate attachment (fits in active site) | 132 | |
| 5272751227 | Noncompetitive inhibition | Molecule attaches enzyme somewhere other than active site changes active site shaping preventing attachment to substrate | 133 |
