AP - Biochemistry Flashcards
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10784124987 | Isotopes | Atoms of the same element that have different numbers of neutrons | 0 | |
10784124988 | Covalent bonds | Bonds created by sharing electrons with other atoms | ![]() | 1 |
10784124989 | Nonpolar covalent bonds | A type of covalent bond in which electrons are shared equally between two atoms of similar electronegativity | ![]() | 2 |
10784124990 | Polar covalent bonds | A type of covalent bond in which electrons are not share equally between 2 atoms; the more electronegative atom pulls electrons closer to itself, making it slightly negative and the other atom slightly positive | ![]() | 3 |
10784124991 | Ionic bonds | Bonds formed when one or more electrons are transferred from one atom to another; The more electronegative atom steals electrons from the less electronegative atom | ![]() | 4 |
10784124992 | Hydrogen bonds | Weak bonds that occurs when a positively charged hydrogen atom in one molecule is attracted to the electronegative atom in another molecule | ![]() | 5 |
10784124993 | Van der Waals Interactions | Weak attractions between molecules or parts of molecules that result from asymmetrical distributions of electors creating temporary partial charges | ![]() | 6 |
10784124994 | Cohesion | An attraction between molecules of the same substance; Example: water molecules sticking to other water molecules | ![]() | 7 |
10784124995 | Adhesion | An attraction between molecules of different substances; Example: water molecules sticking to cellulose | ![]() | 8 |
10784124996 | Surface tension | A measure of how difficult it is to stretch or break the surface of a liquid | ![]() | 9 |
10784124997 | Transpiration | Evaporation of water from the leaves of a plant resulting in the loss of water | ![]() | 10 |
10784124998 | Specific heat | The amount of energy required to raise the temperature of 1 gram of a substance by 1 degree Celsius | 11 | |
10784124999 | Evaporative cooling | The property of a liquid whereby the surface becomes cooler during evaporation, owing to a loss of highly kinetic energy to the gaseous state | ![]() | 12 |
10784125000 | Solution | A homogeneous mixture of two or more substances | 13 | |
10784125001 | Solvent | A liquid substance capable of dissolving other substances | ![]() | 14 |
10784125002 | Solute | A substance that is dissolved in a solution | ![]() | 15 |
10784125003 | Hydrophobic | Water fearing; nonpolar substances that repel water or do not dissolve in water | 16 | |
10784125004 | Hydrophilic | Water loving; polar substances that have a tendency to mix with or dissolve in water | 17 | |
10784125005 | Acid | A substance that increases the hydrogen ion concentration of a solution | 18 | |
10784125006 | Base | A substance that decreases the hydrogen ion concentration in a solution | 19 | |
10784125007 | Buffer | A solution that minimizes changes in pH when acids or bases are added to the solution | 20 | |
10784125008 | Isomer | Compounds with the same chemical formula but different structures | ![]() | 21 |
10784125009 | Dehydration synthesis | A chemical reaction in which two molecules covalently bond to each other with the removal of a water molecule; functions to assemble polymers from monomers | ![]() | 22 |
10784125010 | Hydrolysis | A chemical reaction that breaks bonds between two molecules by the addition of a water molecule; functions in disassembly of polymers to monomers | ![]() | 23 |
10784125011 | Protein | A molecule that is made up of amino acids; contains carbon, hydrogen, oxygen, nitrogen and sulfur | ![]() | 24 |
10784125012 | Peptide Bond | The chemical bond that forms between the carboxyl group of one amino acid and the amino group of another amino acid | ![]() | 25 |
10784125013 | Primary protein structure | The sequence of amino acids in a polypeptide chain | ![]() | 26 |
10784125014 | Secondary protein structure | Hydrogen bonding of the peptide backbone causes the amino acids to fold into a repeating pattern; alpha helix and beta pleated sheet | ![]() | 27 |
10784125015 | Tertiary protein structure | Interactions between side chains of amino acids; results in H bonds, ionic bonds, disulfide bridges, hydrophobic interactions, covalent bonds, etc. | ![]() | 28 |
10784125016 | Quaternary protein structure | Association between two or more polypeptide chains within one protein | ![]() | 29 |
10784125017 | Denatured | Loss of a protein's or enzyme's normal shape so that it no longer functions; usually caused by a change in pH or temperature | ![]() | 30 |
10784125018 | Nucleic Acid | A molecule that is made up of nucleotides; contains carbon, hydrogen, oxygen, nitrogen and phosphorus | ![]() | 31 |
10784125019 | Nucleotide | Monomer of DNA and RNA; consists of a sugar, a phosphate group and a nitrogenous base | ![]() | 32 |
10784125020 | DNA | A double stranded nucleic acid that stores hereditary information; deoxyribonucleic acid | ![]() | 33 |
10784125021 | Carbohydrate | A molecule that is made up of saccharide subunits; contains carbon, hydrogen and oxygen | ![]() | 34 |
10784125022 | Glycosidic linkage | The covalent bond that forms between two monosaccharides | ![]() | 35 |
10784125023 | Lipid | A molecule that is made up of saccharide subunits; contains carbon, hydrogen and oxygen | ![]() | 36 |
10784125024 | Saturated fats | Fatty acid chains that lack double bonds; since the chains are tightly packed, they are solid at room temperature | ![]() | 37 |
10784125025 | Unsaturated fats | Fatty acid chains that contain 1 or more double bonds; since the chains are not tightly packed, they are liquid at room temperature | ![]() | 38 |
10784125026 | Enzyme | A protein that acts as a biological catalyst, which speeds up a chemical reaction in a living organisms | 39 | |
10784125027 | Catabolic pathway | A metabolic pathway that releases energy by breaking down complex molecules to simpler compounds | ![]() | 40 |
10784125028 | Anabolic pathway | A metabolic pathway that consumes energy to synthesize a complex molecule from simpler compounds | ![]() | 41 |
10784125029 | Cofactor | Non-protein helpers that are required for proper enzyme function; Examples: Zn, Fe, Cu | ![]() | 42 |
10784125030 | Coenzyme | An organic molecule serving as a cofactor; required for proper enzyme function; Example: vitamins | ![]() | 43 |
10784125031 | Competitive inhibitor | A substance that reduces the activity of an enzyme by binding to the enzyme's active site in place of the substrate; competitive inhibitor mimic the structure of the enzyme's substrate | ![]() | 44 |
10784125032 | Noncompetitive inhibitor | A substance that reduces the activity of an enzyme by binding to a location apart from the active site, changing its shape so that it no longer binds to the substrate | ![]() | 45 |
10784125033 | Allosteric regulation | When a protein's function at one site is affected by the binding of a regulatory molecule at a separate site | ![]() | 46 |
10784125034 | Feedback inhibition | A method of metabolic control in which the end product of a metabolic pathway acts as an inhibitor of an enzyme within that pathway | ![]() | 47 |