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AP Biology Unit 1

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88137966bicarbonate-carbonic acid buffer systembuffering system that controls the pH of human blood
88137967acid precipitationrain, snow, or fog with a pH lower than 5.2; caused by sulfur and nitrous oxides, which are byproducts of burning fossil fuels
88137968vitalismbelief in a life force outside the jurisdiction of physical and chemical laws; disproved with beginning of abiotic synthesis of organic compounds
88137969ureaorganic compound found in animals' urine: CO(NH2)2; first synthesized by Wöhler
88137970mechanismphysical and chemical laws govern all natural phenomena; made popular because of Miller's abiotic synthesis experiment with primeval sea water
88137971hydrocarbonsorganic molecules consisting of only carbon and hydrogen; nonpolar bonds between C and H produce hydrophobic molecules; undergo reactions that produce lots of energy (like gasoline and fats)
88137972cison the same side
88137973transon the opposite side
88137974enantiomersisomers that are mirror images of each other; usually one is biologically active while the other is not
88137975thalidomidemedication proscribed in the 50s and 60s; example of an enantiomer; one relieves morning sickness, the other causes severe birth defects
88137976steroidsorganic molecule characterized by a carbon skeleton in the form of four fused rings; vary in chemical groups attached to them
88137977hydroxylfunctional group -OH; forms alcohols; polar and hydrophilic
88137978carbonylfunctional group >CO; forms ketones (if in the middle of carbon skeleton) and aldehydes (if at the end); these two groups form sugars (aldoses and ketoses); hydrophilic
88137979carboxylfunctional group -COOH; forms carboxylic acids; has acidic properties (charge of 1- in cells); hydrophilic
88137980aminofunctional group -NH2; forms amines, which form amino acids; has basic qualities (charge of 1+ in cells); hydrophilic
88137981amino acidscompounds with both carboxyl and amino functional groups; at center is alpha carbon, partnered with H, -NH2, -R, -COOH
88137982sulfhydrylfunctional group -SH; forms thiols; when two react together (cross-link), they help stabilize proteins (e.g., in hair); hydrophilic
88137983phosphatefunctional group -OPO3^2-; forms organic phosphates, which are the backbone for phospholipids; hydrophilic; reacts with water, releasing energy
88137984methylfunctional group -CH3; forms methylated compounds, which can affect expression of genes (e.g., testosterone vs. estradiol); hydrophobic
88137985ATPadenosine triphosphate; when reacts with water, becomes ADP: this reaction releases energy which can be used in a cell
88137986macromoleculeshuge, complex organic molecules
88137987polymersmolecule made of a long chain of monomers; formed by condensation/dehydration, broken by hydrolysis
88150716enzymesmacromolecules that facilitate chemical reactions (mostly proteins); speed up dehydration when forming polymers, and hydrolysis during digestion
88150717carbohydrateslarge biological compounds; include sugars (3 to 7 carbons long) and polymers of sugars; often form rings
88150718monosaccharidessimple sugar; have structural formulas that are multiples of CH2O; source of cell nutrients and raw material for forming amino acids, fatty acids, etc.
88150719glucosemost common monosaccharide; can form aldoses or ketoses, depending on location of carbonyl group (glucose: aldose; fructose: ketose)
88150720glycosidic linkagecovalent bond between two monosaccharides that forms disaccharides using dehydration
88150721maltoseglucose+glucose linked by glycosidic linkage; used in brewing beer
88150722sucroseglucose+fructose linked by glycosidic linkage; table sugar
88150723lactoseglucose+galactose linked by glycosidic linkage; in milk
88150724starchpolysaccharide stored in plants (made of alpha glucose) within plastids; hydrolyzed when energy needed
88161855glycogenpolymer of glucose found in animals' liver and muscle cells; like amylopectin (branched plant starch), but more extensively branched; quickly used up if not supplemented by food intake
88161856cellulosestructural polysaccharide; form plant cell walls; polymer of beta glucose; these long, unbranched chains form microfibrils
88161857chitincarbohydrate used by anthropods to form their exoskeletons; flexible when pure, but when exposed to calcium carbonate, hardens; also found in fungi (functions similarly to cellulose)
88161858lipidstoo small to be called macromolecules; hydrophobic, because they consist mostly of nonpolar hydrocarbons; three types: fats, phospholipids, steroids
88161859fatsformed with glycerol (three carbons, each with -OH group) and fatty acids (16-18 carbons long, with carboxyl group at the end); formed by ester linkages
88161860ester linkagebond between hydroxyl and carboxyl; used when forming fats
88161861triacylglycerol3 fatty acids linked to one glycerol molecule
88199776phospholipidsmake up cell membranes; has two fatty acids attached to glycerol; third hydroxyl in glycerol is attached to phosphate; form bilayers in water, because tail is hydrophobic and head is hydrophilic; this is how cell membranes are formed
88199777cholesterolcomponent of cell membranes; help make steroids; synthesized in livers of vertebrates
88199778polypeptidespolymers of amino acids; one or more makes a protein
88199779peptide bondcovalent bond between amino group of one amino acid and carboxyl group of another; formed by dehydration; produces polypeptides
88199780N-terminusamino group at the end of a polypeptide
88199781C-terminuscarboxyl group at the end of a polypeptide
88199782proteinformed from polypeptides and folded according to the bonds, which depend on the sequence of amino acids that make up the polypeptides; two kinds: globular and fibrous
88221731primary structureunique sequence of amino acids in a polypeptide chain of a protein
88221732secondary structurecoiling (alpha helix) or folding (beta pleated sheet) that polypeptide chains take on as a result of the hydrogen bonds between the repeating amino acids in the polypeptide backbone
88221733alpha helixform of secondary structure in polypeptide chains; H-bond is present between every fourth amino acid
88221734beta pleated sheetform of secondary structure in poly peptide chains; two parts of the chain lie side by side, and H-bonds form between them; make up many globular proteins and some fibrous proteins
88221735tertiary structureoverall shape of polypeptide; results from interactions between side chains of amino acids
88221736hydrophobic interactioncontributes to formation of tertiary structure of proteins: amino acids with hydrophobic side chains are put at the core; held together by van der Waals interactions
88221737disulfide bridgestwo cysteine amino acids (have -SH groups on side chains) brought close together, and forms -S-S- bridge; keeps part of the polypeptide back bone together
88221738quaternary structureaggregation of polypeptides; happens when a protein is made up of more than one polypeptide
88221739hemenonpolypeptide component found in hemoglobin; iron atom that binds oxygen
88231383denaturationunraveling of a protein, because it is not in its natural environment, or because it is exposed to a chemical that disrupts H-bonds, ionic bonds and/or disulfide bridges; also excessive heat; sometimes can renature when denaturing agent is removed
88231384chaperoninsprotein molecules that assist in the proper folding on other proteins; protects polypeptide while it folds
88231385X-ray crystallographydetermines 3-D structures of proteins; first used for hemoglobin; NMR spectroscopy and bioinformetics also used to view/predict protein structures
88231386nucleic acidscompounds including DNA and RNA
88231387deoxyribonucleic acidinherited genetic material; usually comprised of several hundred genes; each molecule of DNA makes up a chromosome; programs functions, but does not directly make cells function (proteins do that)
88270970ribosomescenters of protein synthesis; mRNA conveys genetic information from nucleus to cytoplasm, and ribosomes assemble polypeptides using that information
88270971polynucleotidesnucleic acids (which exist as polymers); consist of nucleotides
88270972nucleotidemake up polynucleotides; 3 parts: nitrogenous base, pentose, and phosphate group
88270973nucleosidepart of nucleotide without phosphate group
88270974pyrimidines6-membered ring of carbon and nitrogen atoms; cytosine (C), thymine (T), and uracil (U)
88270975purines6-membered ring fused to 5-membered ring; adenine (A) and guanine (G)
88270976guanine, cytosine, adeninemembers that make up nitrogenous bases in both DNA and RNA
88270977uracilfound only in RNA
88270978thyminefound only in DNA
88270979ribose/deoxyribosesugar connected to nitrogenous base in nucleotides of RNA/DNA; deoxyribose lacks an oxygen; have ' (prime) to distinguish them from nitrogenous bases
88270980phosphodiester linkageconnects phosphate to the sugars of two nucleotides
88270981antiparallelarrangement of DNA polynucleotide strands in their double helix formation; strands held together by hydrogen bonds between nitrogenous bases
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