A review of all of the Campbell 7th Edition terms for the new 2013 AP Biology Curriculum
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| 5216002031 | polar | Molecule with partial charges. Mixes with water. |  | 0 |
| 5216002032 | nonpolar | No partial charges. Do not mix with water. |  | 1 |
| 5216002033 | electronegativity | Attraction of an atom for electrons in a covalent bond. |  | 2 |
| 5216002034 | cohesion | Water molecules sticking to each other. |  | 3 |
| 5216002035 | adhesion | Water molecules sticking to other surfaces. |  | 4 |
| 5216002036 | solute | Something dissolved in a solution. |  | 5 |
| 5216002037 | solvent | Dissolving agent of a solution. |  | 6 |
| 5216002038 | isomers | Same atoms but different arrangement. |  | 7 |
| 5216002039 | structural isomers | Differ in arrangement of atoms. |  | 8 |
| 5216002040 | geometric isomer | Differ in arrangement around a double bond. |  | 9 |
| 5216002041 | enantiomers | Structures that are like a mirror-image. |  | 10 |
| 5216002042 | alpha glucose | Monomer for starch and glycogen. |  | 11 |
| 5216002043 | beta glucose | Monomer for cellulose and chitin. |  | 12 |
| 5216002044 | cellulose | Carbohydrate component of plant cell walls. |  | 13 |
| 5216002045 | starch | Storage polysaccharide of plants. |  | 14 |
| 5216002046 | glycogen | Extremely branched polymer of glucose. |  | 15 |
| 5216002047 | chitin | Polysaccharide found in arthropod exoskeletons and fungal cell walls. |  | 16 |
| 5216002048 | -ose | Suffix of a sugar. |  | 17 |
| 5216002049 | Triglyceride (tryiacylglycerol) | fat molecules composed of three parts fatty acids and one part glycerol |  | 18 |
| 5216002050 | steroids | Made of four rings of carbon. Lipids that act as chemical messengers |  | 19 |
| 5216002051 | cholesterol | Steroid common in cell membranes, also in many hormones. |  | 20 |
| 5216002052 | peptide bond | Bonds that connect amino acids. |  | 21 |
| 5216002053 | disulphide bridges | Reinforce tertiary structure. |  | 22 |
| 5216002054 | primary structure | Order of amino acids in a protein. |  | 23 |
| 5216002055 | secondary structure | Three-dimensional form of segments of protein. Examples are alpha helix or beta pleated sheet. |  | 24 |
| 5216002056 | tertiary structure | Three-dimensional structure of a single polypeptide chain. |  | 25 |
| 5216002057 | quaternary structure | Three-dimensional structure of proteins made of multiple polypeptide subunits. |  | 26 |
| 5216002058 | purines | Bases with a double-ring structure. Adenine & Guanine |  | 27 |
| 5216002059 | pyrimidines | Bases with a single-ring structure. thymine and cytosine |  | 28 |
| 5216002060 | phosphodiester bonds | Bonds between phosphate group and pentose sugar in nucleic acids. |  | 29 |
| 5216002061 | synthesis | To put together. |  | 30 |
| 5216002062 | digestion | To break apart. |  | 31 |
| 5216002063 | dehydration synthesis | Condensation reaction where molecules are connected by loss of a water molecule. |  | 32 |
| 5216002064 | hydrolysis | Reaction where water split into two hydrogens and one oxygen; this breaks a polymer. |  | 33 |
| 5216002065 | anabolism | Metabolic pathways that construct molecules, requiring energy. |  | 34 |
| 5216002066 | catabolism | Metabolic pathways that break down molecules, releasing energy. |  | 35 |
| 5216002067 | transport protein | A membrane protein, specifically a transport protein, that has a hydrophilic channel that certain molecules or atomic ions use as a tunnel. |  | 36 |
| 5216002068 | channel protein | A membrane protein, specifically a transport protein, that has a hydrophilic channel that certain molecules or atomic ions use as a tunnel. |  | 37 |
| 5216002069 | aquaporin | A membrane protein, specifically a transport protein, that facilitates the passage of water through channel proteins. |  | 38 |
| 5216002070 | carrier protein | A membrane protein, specifically a transport protein, that holds onto molecules and changes their shapes in a way that shuttles them across the membrane. |  | 39 |
| 5216002071 | protein kinase | The enzyme that transfers phosphate groups from ATP to protein. |  | 40 |
| 5216002072 | ATP (adenosine triphosphate) | Composed of a sugar ribose, nitrogenous base adenine, and a chain of three phosphate groups bonded to it. |  | 41 |
| 5216002073 | phosphorylation | The metabolic process of introducing a phosphate group into an organic molecule. |  | 42 |
| 5216002074 | catalyst | A chemical agent that speeds up a reaction without being consumed by the reaction. |  | 43 |
| 5216002075 | enzyme | A catalytic protein. Speeds up reactions |  | 44 |
| 5216002076 | activation energy | The amount of energy needed to push the reactants over an energy barrier. |  | 45 |
| 5216002077 | enzyme-substrate complex | When an enzyme binds to its substrate, it forms: |  | 46 |
| 5216002078 | active site | A pocket or groove on the surface of the enzyme. |  | 47 |
| 5216002079 | induced fit | Brings chemical groups of the active site into positions that enhance their ability to catalyze the chemical reaction. |  | 48 |
| 5216002080 | cofactor | Non-protein helpers that may be bound tightly to the enzyme as a permanent resident, or may bind loosely and reversibly along with the substrate. |  | 49 |
| 5216002081 | coenzyme | If the cofactor is an organic molecule. |  | 50 |
| 5216002082 | competitive inhibitors | Reduce the productivity of enzymes by blocking substrates from entering active sites. |  | 51 |
| 5216002083 | noncompetitive inhibitors | Impede enzymatic reactions by binding to another part of the enzyme (other than the active site). |  | 52 |
| 5216002084 | allosteric regulation | When a protein's function at one site is affected by the binding of a regulatory molecule to a separate site. |  | 53 |
| 5216002085 | cooperativity | It amplifies the response of enzymes to substrates. |  | 54 |
| 5216002086 | feedback inhibition | A metabolic pathway is switched off by the inhibitory binding of its end product to an enzyme that acts early in the pathway. |  | 55 |
| 5216002087 | hydrophilic | water-loving |  | 56 |
| 5216002088 | hydrophobic | Water fearing |  | 57 |
| 5216002089 | surface tension | A measure of how difficult it is to stretch or break the surface of a liquid. Water has a high surface tension because of the hydrogen bonding of surface molecules. The result of an inward pull among the molecules of a liquid that brings the molecules on the surface closer together |  | 58 |
| 5216002090 | capillary action | A proccess powered by adhesion that causes water molecules to move upward through a narrow tube such as the stem of a plant. |  | 59 |
| 5216002091 | functional group | the portion of a molecule that is active in a chemical reaction and that determines the properties of many organic compounds |  | 60 |
| 5216002092 | hydroxyl group |  | 61 | |
| 5216002093 | carboxyl group |  | 62 | |
| 5216002094 | amino group | | 63 | |
| 5216002095 | phsophate |  | 64 | |
| 5216002096 | methyl |  | 65 | |
| 5216002097 | saturated fat | A lipid made from fatty acids that have no double bonds between carbon atoms and is solid at room temperature. |  | 66 |
| 5216002098 | unsaturated fat | A fat derived from plant and some animal sources, especially fish, that is liquid at room temperature and whose fatty acid chains contain at least one double bond. |  | 67 |
| 5216002099 | phospholipid | A molecule that is a constituent of the inner bilayer of biological membranes, having a polar, hydrophilic head and a nonpolar, hydrophobic tail. |  | 68 |
| 5216002100 | denatured | An uncoiled, or unraveled protein, the protein has lost its shape due to high temperatures or strong chemicals, its weak bonds have broken and the protein cannot perform its job, since it no longer "fits" with other molecules |  | 69 |
| 5235641909 | Enzymes are part which macromolecule group? | Proteins | 70 | |
| 5235648167 | Enzymes make products from reactants. Reactants that work with enzymes are called... | substrates | 71 | |
| 5235650935 | Where does a substrate bind to an enzyme? | active site | 72 | |
| 5235658461 | What is not a way enzymes work to speed up reactions? | Enzymes remove their own H & OH to give water to reactions | 73 | |
| 5235661345 | Enzymes rate of production can be affected by all the below except | Concentration of nutrients | 74 | |
| 5235664948 | An enzyme is denatured when... | It's shape has changed | 75 | |
| 5235668429 | There are two ways to describe data collected, observations are ...... and measurements are ... | Qualitative....Quantitative | 76 | |
| 5235671175 | Which of the following statements correctly describe(s) catabolic pathways? | They release energy as they degrade polymers to monomers | 77 | |
| 5235673997 | Which of the following is true for all exergonic reactions? | The reaction proceeds with a net release of free energy | 78 | |
| 5235679565 | Which of the following underlie all types of enzyme regulation? | Changes in the active site of the enzyme Changes in the activation energy of the reaction | 79 | |
| 5235686035 | How does a non-competitive inhibitor decrease the rate of an enzyme reaction? | By changing the structure of the enzyme | 80 |
