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AP Biology Unit 1 Vocabulary Review Flashcards

A review of all of the Campbell 7th Edition terms for the new 2013 AP Biology Curriculum

Terms : Hide Images
2789582161polarMolecule with partial charges. Mixes with water.0
2789582162nonpolarNo partial charges. Do not mix with water.1
2789582163electronegativityAttraction of an atom for electrons in a covalent bond.2
2789582164cohesionWater molecules sticking to each other.3
2789582165adhesionWater molecules sticking to other surfaces.4
2789582166soluteSomething dissolved in a solution.5
2789582167solventDissolving agent of a solution.6
2789582168isomersSame atoms but different arrangement.7
2789582169structural isomersDiffer in arrangement of atoms.8
2789582170geometric isomerDiffer in arrangement around a double bond.9
2789582171enantiomersStructures that are like a mirror-image.10
2789582172alpha glucoseMonomer for starch and glycogen.11
2789582173beta glucoseMonomer for cellulose and chitin.12
2789582174celluloseCarbohydrate component of plant cell walls.13
2789582175starchStorage polysaccharide of plants.14
2789582176glycogenExtremely branched polymer of glucose.15
2789582177chitinPolysaccharide found in arthropod exoskeletons and fungal cell walls.16
2789582178-oseSuffix of a sugar.17
2789582179tryiacylglycerolGlycerol and three fatty acids.18
2789582180steroidsMade of four rings of carbon.19
2789582181cholesterolSteroid common in cell membranes, also in many hormones.20
2789582182peptide bondBonds that connect amino acids.21
2789582184disulphide bridgesReinforce tertiary structure.22
2789582185primary structureOrder of amino acids in a protein.23
2789582186secondary structureThree-dimensional form of segments of protein. Examples are alpha helix or beta pleated sheet.24
2789582187tertiary structureThree-dimensional structure of a single polypeptide chain.25
2789582188quaternary structureThree-dimensional structure of proteins made of multiple polypeptide subunits.26
2789582190purinesBases with a double-ring structure.27
2789582191pyrimidinesBases with a single-ring structure.28
2789582192phosphodiester bondsBonds between phosphate group and pentose sugar in nucleic acids.29
2789582193synthesisTo put together.30
2789582194digestionTo break apart.31
2789582195dehydration synthesisCondensation reaction where molecules are connected by loss of a water molecule.32
2789582196hydrolysisReaction where water split into two hydrogens and one oxygen; this breaks a polymer.33
2789582197anabolismMetabolic pathways that construct molecules, requiring energy.34
2789582198catabolismMetabolic pathways that break down molecules, releasing energy.35
2789582514transport proteinA membrane protein, specifically a transport protein, that has a hydrophilic channel that certain molecules or atomic ions use as a tunnel.36
2789582515channel proteinA membrane protein, specifically a transport protein, that has a hydrophilic channel that certain molecules or atomic ions use as a tunnel.37
2789582516aquaporinA membrane protein, specifically a transport protein, that facilitates the passage of water through channel proteins.38
2789582517carrier proteinA membrane protein, specifically a transport protein, that holds onto molecules and changes their shapes in a way that shuttles them across the membrane.39
2789582539protein kinaseThe enzyme that transfers phosphate groups from ATP to protein.40
2789582620ATP (adenosine triphosphate)Composed of a sugar ribose, nitrogenous base adenine, and a chain of three phosphate groups bonded to it.41
2789582621phosphorylationThe metabolic process of introducing a phosphate group into an organic molecule.42
2789582622catalystA chemical agent that speeds up a reaction without being consumed by the reaction.43
2789582623enzymeA catalytic protein.44
2789582624activation energyThe amount of energy needed to push the reactants over an energy barrier.45
2789582625enzyme-substrate complexWhen an enzyme binds to its substrate, it forms:46
2789582626active siteA pocket or groove on the surface of the enzyme.47
2789582627induced fitBrings chemical groups of the active site into positions that enhance their ability to catalyze the chemical reaction.48
2789582628cofactorNon-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
2789582629coenzymeIf the cofactor is an organic molecule.50
2789582630competitive inhibitorsReduce the productivity of enzymes by blocking substrates from entering active sites.51
2789582631noncompetitive inhibitorsImpede enzymatic reactions by binding to another part of the enzyme (other than the active site).52
2789582632allosteric regulationWhen a protein's function at one site is affected by the binding of a regulatory molecule to a separate site.53
2789582633cooperativityIt amplifies the response of enzymes to substrates.54
2789582634feedback inhibitionA metabolic pathway is switched off by the inhibitory binding of its end product to an enzyme that acts early in the pathway.55

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