| 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 |