| Term | Definition |
|---|
| molecules | Structures made up of two or more atoms |
| compound | Made of at least 2 different atoms |
| Ionic Bonding | this type of bonding forms when the outermost, or valence, electrons of an atom are donated or received in association with a second atom |
| Covalent Bonding | Sharing of electrons so each atom has a complete outer shell |
| Organic molecules | all consist of carbon atoms, Carbon-based molecules |
| Oxidation reactions: Ionic | refers to a loss of electrons |
| Oxidation reactions: Covalent | refers to a loss of hydrogen atoms |
| Reduction reactions: Ionic | refers to a gain of electrons |
| Reduction reactions: Covalent | refers to a gain of hydrogen ions |
| Hydrogen Bond | a weak chemical bond found between molecules, where one molecule has a covalently bonded hydrogen |
| Cohesion: for water | water bonded to water; creates surface tension, raindrops, allows things to get wet |
| Adhesion: for water | Water bonded to other charged compounds. Acts as lubricants, allows things to get wet. Ex. This can be seen in the capillary action where water is "pulled up" in the xylem of plants. |
| lattice shape | Ex. ICE: Hydrogen bonds become fixed and form this space which leaves large spaces between molecules |
| Hydrophobic | non-charged molecules which don't attract water. "water-hating" ex. plasma membrane |
| Hydrophylic | charged molecules that are attracted to water "water-loving" |
| Mixture | 2 or more substances combine w/o forming bonds with eachother |
| Solutions | Are mixtures that have combined molecules that are equally distributed throughout |
| pH | stands for "potential hydrogen" A scale used to indicate the acidity |
| pH<7 | acid |
| acids | molecules that dissociate in water, releasing protons H+ |
| pH=7 | neutrality |
| Bases | turns red litmus paper blue; are substances that dissociate in water (OH-) |
| ph>7 | base |
| Salts | acids and bases can neutralize eachother to produce water and salt |
| Buffers | Are combinations of a weak acid and its salt, and has the effect of stabilizing the pH of a solution. Even if strong acids/bases are added the pH will not change dramatically |
| Protein buffer System | found in all tissues |
| Phosphate buffer System | found in kidneys and intracellular fluid |
| water molecule | A polar molecule |
| Organic molecules | always contain carbon and hydrogen atoms |
| Carbon | 4 electrons in outer shell. Helps form strong colvalent bonds and double/triple bonds with itself |
| Functional groups | can attatch to carbon chains ex. carboxyl COOH |
| Isomers | Variation in covalent arrangement. Same formulas-but different shape and functions |
| structural: isomer shape | linear shape |
| geometric: isomer shape | around a double bond |
| enentiomers: isomer shape | mirror images of eachother right-handed and left-handed |
| Organic molecules: 4 classes | 1. Carbohydrates 2. Lipids 3. Proteins 4. Nucleic Acids |
| Macromolecule | a very large organic molecule, usually a polymer, composed of hundreds or thousands of atoms |
| monomers | small molecules/subunits |
| polymer | made up of monomers linked/bonded together |
| Dehydration Synthesis | "condensation synthesis" extraction/loss of water molecule |
| Hydrolysis | Water is added to the molecule to break the polymers into monomers |
| Carbohydrates | Elements: C,H,O. 1:2:1 identify by the ending "ose"--- a main source of energy |
| Monosaccharides | one/simple sugar |
| Disaccharides | 2 sugars- created by dehydration synthesis |
| sucrose | (table sugar) glucose + fructose |
| lactose | milk sugar, glucose + galactose |
| maltose | glucose + glucose |
| Polysaccharides | A long chain of monosaccharides |
| Glycogen | form in which animals for carbohydrates: like amylopectin except its branching only includes 16-24 glucose units |
| Lipids | Are a diverse group of compounds that mainly consist of carbon and hydrogen atoms linked by non-polar covalent bonds |
| Lipids: 4 kinds | 1. Fats/Oils 2. Phospholipids 3. Waxes 4. Steroids |
| Fats/Oils: 3 Functions in animals | 1. long-term energy storage 2. insolation against heat loss 3. forms protective cushion around organs |
| triglyceride | Fats/Oils: structure: 1 glycerol + 3 fatty acids --> fat + 3 water "tri-glyceride" --reffered to as "neutral fat" due to its non-polar nature |
| Fatty acids | consist of a 16-18 atom carbon chain ending with an acid group COOH |
| Saturated Fat | straight chains; fat in which all three fatty acid chains contain the maximum possible number of hydrogen atoms |
| Unsaturated Fat | Fatty acids which have carbon atoms connected by double bonds---butter, lard |
| Polyunsaturated Fat | The fatty acid contains more than one double carbon bond ex. corn/olive/peanut/sunflower oil--will not solidify at room temperature |
| Phospholipids | major component of all membranes. Hydrophobic tail: 2 fatty acid chains (non-polar). Hydrophylic head: In place of the 3rd fatty acid chain there is a phosphate group(ing) that has both phosphate and nitrogen (which is polar) |
| waxes | One fatty acid linked to an alcohol; more hydrophobic than fats |
| steroids | ipids characterized by a carbon skeleton consisting of four fused rings: 3 hexagons + 1 pentagon |
| Cholesterol | (under steroids) common in animal cell membranes starting material for estrogen and testosterone |
| Proteins | Each one of us has tens of thousands. A biological polymer constructed from amino acid monomers. |
| 5 elements in proteins | 1. Carbon 2. Hydrogen 3. Oxygen 4. Nitrogen many times 5. Sulfur |
| Amino acid | A central carbon covalently to: 1. Amino group NH2 2. carboxyl (acid) group COOH 3. Hydrogen 4. "R" chemical group variable of the amino acid |
| peptide bond | covalent bond that joins 2 amino acids together (polar) |
| dipeptide | 2 amino acids bonded together |
| polypeptide | more than 2 amino acids joined together (single chain of amino acids), a protein is eventually formed with 75 or more joined amino acids |
| Primary structure: protein | amino acids in linear order, for the protein to function, it must have the correct collection of amino acids arranged in precise order ex. amino acid changes in hemoglobin: result is sickle cell anemia |
| Secondary structure: protein | the regular coiling/folding of a polypeptide created by hydrogen bonding--hydrogen bonding between N-H and C-O groups will produce an alpha helix or a pleated sheet shape |
| Tertiary structure: protein | "overall 3D shape" --either globular/fibrous. Held in shape by hydrogen bonding or sulfur bonds between amino acids called a disulfide bridge |
| Disulfide bridge | in the protein tertiary structure. It hold the amino acids in shape |
| Quaternary structure: protein | The shape when the protein consists of 2 or more polypeptide chains (or subunits) linked together, the subunits may be identical or different ex. hemoglobin: 4 subunits of 2 distinct types |
| denaturation | For proteins, a process in which a protein unravels and loses its native conformation, thereby becoming biologically inactive. For DNA, the separation of the two strands of the double helix. Denaturation occurs under extreme conditions of pH, salt concentration, and temperature. |
| coagulation | change in protein is permenant, and it will not return to its normal shape or ability to function |
| Enzymatic proteins | Selective acceleration of chemical reactions ex. digestive enzymes hydrolyze the polymers in food |
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