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LHS AP Bio 1
LHS AP Bio Biochemistry Review
| Question | Answer |
|---|---|
| Ionic bonds | bonds when electrons are transferred; typically between metals and nonmetals |
| Covalent bonds | bonds that form when electrons are shared; typically between nonmetals |
| Nonpolar covalent bonds | bonds that form when electrons are shared equally |
| Hydrogen bonds | positively charged hydrogen atom in one covalent molecule is attracted to a negatively charged area of another |
| Hydrophobic | nonpolar covalent substances that do not dissolve in water; “water fearing” |
| Hydrophillic | polar substances; “water loving” |
| Heat capacity | the degree to which a substance changes temperature in response to a gain or loss of heat |
| Cohesion | the attraction between like substances |
| Adhesion | the attraction of unlike substances |
| capillary action | when water adheres to the walls of narrow tubing or to absorbent solids like paper |
| Organic molecules | have carbon atoms |
| Macromolecules | consist of hundreds or thousands of atoms |
| Polymer | a single unit repeated many times |
| Monomer | a single unit |
| monosaccharide | a single sugar molecule |
| disaccharide | two sugar molecules joined by a glycosidic linkage |
| dehydration synthesis | The chemical process by which a molecule of water is removed from the reactants to join the reactants together |
| polysaccharide | a series of connected monosaccharides |
| Starch | a polymer of alpha glucose molecules produced by plants |
| Glycogen | a polymer of alpha glucose molecules; energy storage molecule in animal cells. |
| Cellulose | a polymer of beta glucose molecules; structural molecule in the walls of plant cells |
| Chitin | polymer of beta glucose molecules with nitrogen |
| Triglycerides | fats and oils, they consist of three fatty acids attached to a glycerol molecule |
| saturated fatty acid | has a single covalent bond between each pair of carbon atoms |
| monounsaturated fatty acid | has one double covalent bond |
| polyunsaturated fatty acid | two or more double covalent bonds |
| phospholipid | a lipid except that has one of the fatty acid chains replaced by a phosphate group |
| amphipathic molecule | has both polar (hydrophilic) and nonpolar (hydrophobic) regions |
| Steroids | have a backbone of four linked carbon rings. Ex. cholesterol and certain hormones |
| Enzymes | globular proteins that act as catalysts for metabolic reactions |
| Defensive proteins | provide protection against foreign substances that enter the bodies of animals |
| Transport proteins | transport materials into and out of cells |
| amino acids | monomers of proteins, consist of an amino group (NH2), a carboxyl group (COOH), and a functional group |
| primary structure | the sequence of amino acids in a protein |
| secondary structure | hydrogen bonding produces a alpha helix and beta pleated sheet |
| tertiary structure | 3D shaping due to interactions between functional groups |
| quaternary structure | structure of a protein assembled from two or more separate peptide chains |
| DNA | deoxyribonucleic acid, a polymer of nucleic acids |
| Nucleotide | consists of three parts: a nitrogen base, a five |
| Adenine | a double ring base (purine) |
| Thymine | a single ring base (pyrimidine) |
| Cytosine | a single ring base (pyrimidine) |
| Guanine | a double ring base (purine) |
| Pyrimidines | single ring nitrogenous base |
| Purines | double ring nitrogenous base |
| RNA | ribonucleic acid |
| Uracil | single ring base (pyrimidine) |
| activation energy | energy required to trigger the formation of new bonds |
| catalyst | accelerates the rate of the reaction by lowering the activation energy |
| metabolism | Chemical reactions that occur in biological systems |
| catabolism | the breakdown of substances |
| anabolism | the formation of new products (synthesis) |
| substrate | the substance or substances upon which the enzyme acts |
| induced fit model | The active site binds to the substrate, causes the enzyme to change shape which results in a change in substrate |
| Cofactors | nonprotein molecules that assist enzymes |
| Coenzymes | organic cofactors that usually function to donate or accept some component of a reaction. |
| Inorganic cofactors | often metal ions, like Fe2+ and Mg2+ |
| ATP | (adenosine triphosphate) a common source of energy for metabolism, basically an adenine and 3 phosphate groups |
| Phosphorylation | when a molecule combines with a phosphate group using energy |
| Allosteric enzymes | have two kinds of binding sites; one an active site for the substrate and one for an allosteric effector. |
| allosteric activator | binds to the enzyme and induces the enzyme’s active form |
| allosteric inhibitor | binds to the enzyme and induces the enzyme’s inactive form |
| feedback inhibition | an end product acts as an allosteric inhibitor, shutting down one of the enzymes |
| competitive inhibition | mimics the substrate occupies the active site and prevents the enzyme from catalyzing the substrate |