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Bio: Chap. 1
Scientific method, cycles, macromolecules, atoms/atom structure
| Question | Answer |
|---|---|
| 1. Scientific Method | 1. Observation, Question, Hypothesis, Prediction, Experimental Design, Data,Analysis |
| 2. Independent Variable | The variable that is manipulated |
| 3. Dependent Variable | The variable that changes in response to the IV |
| 4. Control Variable | A variable that stays the same throughout the experiment |
| 5. Hypothesis vs Prediction | A hypothesis offers an answer with reasoning; a |
| prediction is an if-then (IV-DV) statement 6. Claim-Evidence-Reasoning | Claim |
| 7. Homeostasis | The equilibrium of the body (Ex. Sweating; Heart rate changes) |
| 8. Characteristics of living things | •homeostasis •made up of at least one cell organization,energy use,evolution, reproduction |
| 9. Common biological elements | •Carbon, Hydrogen, Oxygen,Nitrogen |
| 10. Atom | The smallest unit of matter that retains the properties of an element |
| 11. Location of Protons, Neutrons, and Electrons | •Electrons are found in the orbital levels (electron shells) around the nucleus •Protons and Neutrons are found in the nucleus |
| 12. Atomic number | The number of protons in an atom; determines the element |
| 13. Mass number | The number of protons and neutrons in the nucleus of an atom |
| 14. Intramolecular bonds | Bonds within a molecule (Ex. Covalent and Ionic) |
| 15. Polar covalent bond | A covalent bond with an uneven distribution of charge between atoms (Ex. O-H) |
| 16. Non-polar covalent bond | A covalent bond with an even distribution of charge between atoms (Ex. C-H) |
| 17. Covalent Bond | Electrons are SHARED between atoms |
| 18. Ionic Bond | Electrons are TRANSFERRED from one atom to another |
| 19. Hydrogen Bonds | A weak attraction between polar molecules (containing atoms of hydrogen) |
| 20. Importance of hydrogen bonding in water | Hydrogen bonds are crucial to all emergent properties of water |
| 21. Emergent properties of water | •Cohesion •Adhesion •High Specific Heat •Evaporative Cooling •Density of Water •Solubility •Surface Tension •Polarity |
| 22. Cohesion | Attraction between molecules of the same substance (Ex. H2O and H2O) 23. Adhesion |
| 35. 3 major macromolecules | Carbohydrates, Lipids, Proteins |
| 36. Carbohydrates | Includes sugars and the polymers of sugars; hydrophilic (C,H,O) |
| 37. Monosaccharides | Single sugar molecules; the monomers of carbs (Ex. Glucose, Fructose, Galactose) |
| 38. Disaccharides | Double sugars; made up of two monosaccharides; the polymers of carbs (Ex. Lactose, Sucrose, Maltose) |
| 39. Polysaccharides | Complex carbohydrates; long chains of sugars with more than two monosaccharides; the polymers of carbs (Ex. Starch, Glycogen, Cellulose) |
| 40. Carbohydrates | Structure and function |
| 41. Lipids | Fats and Steroids; Energy-rich (C,H,O) |
| 42. 1 glycerol + 3 fatty acids | Triglyceride |
| 43. Fatty acids | Long hydrocarbons that store lots of energy |
| 44. Monomers of lipids | Glycerol and fatty acids |
| 45. Polymers of lipids | Triglycerides |
| 46. Saturated fats | Solid at room temperature; Single bonds make fatty acids straight (Ex. Butter) |
| 47. Unsaturated fats | Liquid at room temperature; Double bonds cause bends in fatty acids (Ex. Fish oils) |
| 48. Trans fats | Made by hydrogenating unsaturated fats; not good for you |
| 49. Steroids | A carbon skeleton with four fused rings (Ex. Cholesterol, Testosterone, Estrogen) |
| 50. Anabolic steroids | Synthetic variations of testosterone; causes buildup of muscle and bone mass; abused in sports |
| 51. Function of lipids | Stores energy, provides insulation, cushions organs, hormones |
| 52. Amino Acids | A carbon atom bonded to four covalent partners; the monomer of proteins; 20 different kinds |
| 53. Proteins | A polymer of amino acids (C,H,O,N) |
| 54. Peptide bond | A bond between two amino acids |
| 55. Polypeptide | A long chain of amino acids; polymer of a protein |
| 56. 4 levels of protein structure | Primary, Secondary, Tertiary, Quaternary |
| 57. Primary structure | The sequence of amino acids in a polypeptide chain |
| 58. Secondary structure | Patterns formed by certain stretches of the polypeptide; reinforced by hydrogen bonds (Ex. Alpha Helix, Pleated Sheet |
| 59. Tertiary structure | Secondary structures combined to make a 3-D structure; reinforced by chemical bonds between side groups of amino acids |
| 60. Quaternary structure | Proteins with two or more polypeptides at the tertiary level |
| 61. Denaturation | A process where a protein unravels and loses its specific structure and therefore function; result of changes in pH or oxygen levels |
| 62. Function of Proteins | Muscle movement, Pigments, Cell reproduction, Transport of materials in cells, Cell signals |
| 63. Enzymes | Proteins that speed up chemical reactions |
| 64. Activation energy | The energy required to start a chemical reaction |
| 65. Catalyze | To begin a chemical reaction |
| 66. Substrate | The reactant molecule of an enzyme |
| 67. Active site | A region of the enzyme that binds to the substrate |
| 68. Induced fit | As the substrate binds with the enzyme, the enzyme changes shape slightly to create a snug fit around the substrate |
| 69. Enzyme inhibitors | Prevent the substrate from catalyzing |
| 70. Competitive inhibitors | Bind to the active site of an enzyme, blocking the active site from the substrate |
| 71. Noncompetitive inhibitor | Prevents the substrate from binding with the enzyme by binding to the allosteric site and changing the shape of the active site |
| 72. Allosteric site | A site on an enzyme other than the active site |
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