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| 5371851283 | Carbs | -CHO 1-2-1 -monomer= glucose -polymer= groups of glucose -Bio examples= cell walls of plants: cellulose, chitin -Energy: 4cal/g, 1ST SOURCE |  | 0 |
| 5371851349 | Lipids | -CHO (lots of C's and H's, little O's) -Monomer= fatty acids/ glycerol -polymers= saturated and unsaturated fats -Bio examples= blubber, phospholipid bilayer -Energy: 9cal/g, 2ND SOURCE |  | 1 |
| 5371853413 | Proteins | -CHON -monomer= amino acids -polymer= polypeptides/ protein -Bio examples= hair, muscles, skin -Energy: 4cal/g, LAST SOURCE |  | 2 |
| 5371853414 | Nucleic Acids | -CHONP -monomer= nucleotides -polymer= DNA, RNA -Bio examples= DNA and RNA -Energy: not a source of energy |  | 3 |
| 5371887843 | Primary Structure | amino acids are joined together | 4 | |
| 5372105423 | Primary interaction | Peptide bonds join together amino acids (C-N) | 5 | |
| 5371887844 | Secondary Structure | 3D shape -alpha helix -beta pleated shape |  | 6 |
| 5372126888 | Secondary interaction | H-bond between amine group of one amino acid and the carboxyl group of another- (Hydrogen to oxygen) | 7 | |
| 5371889522 | Tertiary Structure | Complex globular shape due to R-group interactions |  | 8 |
| 5372148887 | Tertiary Interaction | -hydrophobic interactions -van der waals -disulfide bridges (cysteins are attracted to each other) -enzymes hold them together | 9 | |
| 5371889523 | Quaternary Structure | Multiple tertiary structures put together |  | 10 |
| 5372161775 | Function of Enzymes | To lower the activation energy and start the reaction faster | 11 | |
| 5372222662 | Structure of enzymes | -Enzymes have to be specific to its substrate in order to fit -Substrate bonds to enzyme's active site | 12 | |
| 5373454141 | Normal vs. Allosteric | normal= one active site allosteric= more than one active sit | 13 | |
| 5373832546 | catalyzed reaction | 14 | ||
| 5373461433 | Negative feedback | Inhibition stops a biochemical pathway from making product. | 15 | |
| 5373465286 | Competitive Inhibition | -blocks the active site -competitor makes substrate unable to connect with active site | 16 | |
| 5373471816 | Non-competitive Inhibitition | -Binds to allosteric site and causes a conformational change in active site, so substrate can no longer bind | 17 | |
| 5373483807 | Environmental factors that influence enzyme activity | -temperature -pH -substrate concentration (increase substrate= no change in rxn rate) -enzyme concentration (increase enzyme= increase in rxn rate) | 18 | |
| 5373846652 | Exergonic reaction | -reaction is spontaneous -products have less energy -energy is released |  | 19 |
| 5373850744 | Endergonic reaction | -reaction is not spontaneous -reactants have less energy -energy is absorbed |  | 20 |
| 5373814908 | Denaturing enzyme | permanently deforming enzyme -active site no longer the correct shape -acids/bases change the bonding of R-groups in the active site -heat= destroys and changes shape permanently -cold= molecular movements decrease, less substrate/enzyme interaction | 21 | |
| 5373584612 | Hydroxyl | -OH -Polar -Hydrophilic -found in ALL Nucleic Acids |  | 22 |
| 5373598165 | Methal | -CH3 -non-polar -hydrophobic -found in many lipids |  | 23 |
| 5373603719 | Carboxyl | -COOH -polar -hydrophilic -acidic |  | 24 |
| 5373607541 | Carbonyl | -CO -polar -hydrophilic -acidic |  | 25 |
| 5373622975 | Amine | -NH2 -polar -hydrophilic -found in all proteins |  | 26 |
| 5373658924 | Sulfydryl | -SH -polar -hydrophilic -forms disulfide bridges in proteins |  | 27 |
| 5373667817 | Phosphate | -PO4 -polar -hydrophilic -phospholipids -ALL nucleic acids |  | 28 |
| 5373680906 | Dehydration synthesis | putting monomers together to make polymers -creates H20 -forms peptide bonds |  | 29 |
| 5373706567 | Properties of water | -Choesion -Adhesion -Solvent -High specific heat -high vaporization -Density- water is less dense when solid and most dense at 4 degrees C | 30 | |
| 5373786462 | Acids | -pH of below 7 -excess of H+ ions | 31 | |
| 5373786463 | Bases | -pH of above 7 -excess -OH ions | 32 | |
| 5373796196 | Buffers | substances that minimize changes in pH. Accept H+ from solution when they're in excess and donate H+ when they're depleted. -more acidic= H+ ions increasing, moves to left of rxn -more basic= -OH ions increasing, moves to right of rxn | 33 |
