BIOLOGY 10:25.pdf - Organic Compounds Student Worksheet 1 2 3 4 ... - Free Printable

1. Organic compounds are defined as those containing carbon atoms bonded to hydrogen and often other elements like oxygen, nitrogen, sulfur, or halogens.
2. Inorganic compounds generally do not contain carbon-hydrogen bonds; they include salts, metals, minerals, and simple carbon compounds like CO₂ or carbonates.
3. The four main types of organic macromolecules are carbohydrates, lipids, proteins, and nucleic acids.
4. Carbohydrates: Energy source and structural support (e.g., starch, cellulose). Lipids: Long-term energy storage, insulation, cell membranes (e.g., triglycerides, phospholipids). Proteins: Enzymes, structural components, transport, defense (e.g., hemoglobin, collagen). Nucleic Acids: Store and transmit genetic information (e.g., DNA, RNA).
5. Monomers: Small molecules that link together to form polymers. Polymers: Large molecules made of repeating monomer units.
6. Dehydration synthesis: Monomers join by losing a water molecule; hydrolysis: Polymers break down by adding a water molecule.
7. Carbohydrate monomers: Monosaccharides (e.g., glucose). Lipid monomers: Fatty acids and glycerol. Protein monomers: Amino acids. Nucleic acid monomers: Nucleotides.
8. Carbohydrates: C, H, O. Lipids: C, H, O (sometimes P, N). Proteins: C, H, O, N, S. Nucleic acids: C, H, O, N, P.
9. Carbohydrates: Starch (plants), glycogen (animals). Lipids: Triglycerides (fats/oils). Proteins: Hemoglobin, enzymes. Nucleic acids: DNA, RNA.
10. Carbohydrates: Energy storage (glycogen), structure (cellulose). Lipids: Insulation, membrane structure. Proteins: Catalysis (enzymes), movement (muscle). Nucleic acids: Genetic coding, protein synthesis.
11. Amino acids are linked by peptide bonds to form polypeptide chains (proteins).
12. The primary structure is the linear sequence of amino acids in a protein.
13. The secondary structure involves local folding into alpha helices or beta pleated sheets due to hydrogen bonding.
14. Tertiary structure is the overall 3D shape of a single polypeptide chain, stabilized by interactions between R groups.
15. Quaternary structure occurs when multiple polypeptide chains assemble into a functional protein (e.g., hemoglobin).
16. Denaturation disrupts the protein’s 3D structure without breaking peptide bonds, causing loss of function.
17. Nucleotides consist of a phosphate group, a pentose sugar (ribose or deoxyribose), and a nitrogenous base.
18. DNA bases: Adenine (A), Thymine (T), Guanine (G), Cytosine (C). RNA bases: Adenine (A), Uracil (U), Guanine (G), Cytosine (C).
19. DNA is double-stranded with deoxyribose sugar; RNA is usually single-stranded with ribose sugar.
20. DNA stores genetic information; RNA transmits and translates that information for protein synthesis.
21. The central dogma: DNA → RNA → Protein.
22. ATP (adenosine triphosphate) is the primary energy currency of the cell.
23. ATP consists of adenine, ribose, and three phosphate groups.
24. When ATP loses a phosphate group, it becomes ADP and releases energy for cellular work.
25. Enzymes are biological catalysts (usually proteins) that speed up chemical reactions without being consumed.
26. Enzymes lower the activation energy required for a reaction to proceed.
27. Substrate: The molecule upon which an enzyme acts. Active site: The region of the enzyme where substrate binds.
28. Enzyme specificity means each enzyme catalyzes only one specific reaction due to its unique active site shape.
29. Factors affecting enzyme activity: temperature, pH, substrate concentration, enzyme concentration, inhibitors.
30. Competitive inhibitors bind to the active site; noncompetitive inhibitors bind elsewhere and change the enzyme’s shape.
31. Coenzymes are organic cofactors (often vitamins) that assist enzymes in catalysis.
32. Vitamins are essential organic molecules obtained from diet; many serve as precursors to coenzymes.
33. Minerals are inorganic elements required for enzyme function or structural roles (e.g., iron in hemoglobin).
34. Metabolism includes all chemical reactions in a cell, including catabolism (breaking down) and anabolism (building up).
35. Anabolic reactions build complex molecules from simpler ones, requiring energy (e.g., protein synthesis).
36. Catabolic reactions break down complex molecules into simpler ones, releasing energy (e.g., cellular respiration).
37. Cellular respiration converts glucose and oxygen into ATP, CO₂, and water.
38. Photosynthesis uses sunlight to convert CO₂ and water into glucose and oxygen.
39. Autotrophs produce their own food (e.g., plants); heterotrophs consume other organisms for energy.
40. Fermentation is anaerobic respiration that regenerates NAD⁺ for glycolysis without using oxygen.
41. Glycolysis breaks down one glucose molecule into two pyruvate molecules, producing a net gain of 2 ATP and 2 NADH.
42. The Krebs cycle completes the breakdown of pyruvate, producing CO₂, ATP, NADH, and FADH₂.
43. The electron transport chain uses electrons from NADH and FADH₂ to create a proton gradient that drives ATP synthesis.
44. Aerobic respiration yields ~36-38 ATP per glucose; anaerobic respiration (fermentation) yields only 2 ATP.
45. Mitochondria are the sites of aerobic respiration; chloroplasts are the sites of photosynthesis.
46. The plasma membrane regulates what enters and exits the cell via selective permeability.
47. Passive transport moves substances down their concentration gradient without energy (diffusion, osmosis, facilitated diffusion).
48. Active transport moves substances against their concentration gradient using energy (ATP).
49. Endocytosis brings materials into the cell via vesicles; exocytosis expels materials from the cell via vesicles.
50. Homeostasis is the maintenance of stable internal conditions despite external changes.