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| 9917623572 | Hydroxyl | Polar, alcohol |  | 0 |
| 9917623573 | Carbonyl | Polar, Found in sugar, responsible for sugars being so easily dissolved in water |  | 1 |
| 9917623574 | Carboxyl | Acts as an acid, charge of 1- |  | 2 |
| 9917623575 | Amino | Acts as a base, charge of 1+ |  | 3 |
| 9917623576 | Sulfhydryl | Cross-linking covalent bonds help stabilize protein structures |  | 4 |
| 9917623577 | Phosphate | Potential to react with water, releasing energy |  | 5 |
| 9917623578 | Methyl | Affects expression of genes |  | 6 |
| 9917623579 | ATP | Primary energy-transferring molecule in the cell | 7 | |
| 9917623580 | Polymer | A long molecule consisting of many similar building blocks | 8 | |
| 9917623581 | Monomer | Small building block molecules | 9 | |
| 9917623582 | Dehydration Reaction | Occurs when two monomers bond together through the loss of a water molecule -Builds polymers |  | 10 |
| 9917623583 | Hydrolysis | Reverse of the dehydration reaction, breaking down complex molecules by the chemical addition of water -Disassembles polymers |  | 11 |
| 9917623584 | Monosaccharide | (single sugars) have molecular formulas that are usually multiples of CH2O Classified by: - Location of the carbonyl group - Number of carbons in the skeleton | 12 | |
| 9917623585 | Polysaccharide | Polymers of sugars that have storage and structural roles | 13 | |
| 9917623586 | Glycosidic Linkage | A covalent bond formed between two monosaccharides by a dehydration reaction | 14 | |
| 9917623587 | Starch | A storage polysaccharide of plants, consists of entirely glucose monomers; The simplest form is amylase | 15 | |
| 9917623588 | Glycogen | A storage polysaccharide in animals (stored mainly in liver and muscle cells) | 16 | |
| 9917623589 | Cellulose | A structural polysaccharide comprising plant cell walls (glucose polymer with different glycosidic linkages - beta glucose) | 17 | |
| 9917623590 | Lipid | One class of large biological molecules that do not form polymers, have little or no affinity for water, main function is energy storage | 18 | |
| 9917623591 | Saturated Fatty Acid | Have the maximum number of hydrogen atoms possible and no double bonds | 19 | |
| 9917623592 | Unsaturated Fatty Acid | Have one or more double bonds | 20 | |
| 9917623593 | Ester Linkage | How three fatty acids are joined to glycerol, creating a triacylglycerol |  | 21 |
| 9917623594 | Phospholipid | Two hydrophobic fatty acids and a hydrophilic phosphate group are attached to glycerol | 22 | |
| 9917623595 | Steroid | Lipids characterized by a carbon skeleton consisting of four fused rings | 23 | |
| 9917623596 | Polypeptide | Unbranched polymers built from the same set of 20 amino acids | 24 | |
| 9917623597 | Amino acid | Organic molecules with carboxyl and amino groups | 25 | |
| 9917623598 | Peptide bond | The covalent bond between two amino acid units, formed by a dehydration reaction. | 26 | |
| 9917623599 | Primary structure | The sequence of amino acids in a protein, is like the order of letters in a long word Determined by inherited genetic information | 27 | |
| 9917623600 | Secondary structure | Coils and folds result from hydrogen bonds between repeating constituents of the polypeptide backbone Ex: alpha helix, beta pleated sheet | 28 | |
| 9917623601 | Tertiary structure | Determined by interactions between R groups, rather than interactions between the backbone constituents | 29 | |
| 9917623602 | Quaternary structure | Results when two or more polypeptide chains form one macromolecule | 30 | |
| 9917623603 | Denaturation | Loss of a protein's native structure, biologically inactive protein | 31 | |
| 9917623604 | Nucleotide | Monomers of polynucleotides | 32 | |
| 9917623605 | Polynucleotide | Chain of nucleotides that alone or with another such chain makes up a nucleic acid | 33 | |
| 9917623606 | Phosphodiester linkage | The connection in a nucleic acid strand, formed by covalently bonding two nucleotides together | 34 | |
| 9917623607 | Metabolism | The totality of an organism's chemical reactions | 35 | |
| 9917623608 | Catabolic pathway | Release energy by breaking down complex molecules into simpler compounds | 36 | |
| 9917623609 | Anabolic pathway | Consume energy to build complex molecules from simpler ones | 37 | |
| 9917623610 | First law of thermodynamics | Energy can be transferred and transformed, but it cannot be created or destroyed. | 38 | |
| 9917623611 | Free energy | Energy that can do work when temperature and pressure are uniform, as in a living cell | 39 | |
| 9917623612 | Exergonic reaction | Proceeds with a net release of free energy and is spontaneous | 40 | |
| 9917623613 | Endergonic reaction | Absorbs free energy from its surroundings and is nonspontaneous | 41 | |
| 9917623614 | Phosphorylation | The metabolic process of introducing a phosphate group into an organic molecule, how ATP drives endergonic reactions | 42 | |
| 9917623615 | Enzyme | Protein catalyst that speeds up the rate of specific biological reactions | 43 | |
| 9917623616 | Activation energy | The initial energy needed to start a chemical reaction | 44 | |
| 9917623617 | Induced Fit | Brings groups of the active site into positions that enhance their ability to catalyze the reaction | 45 | |
| 9917623618 | Cofactor | Non-protein enzyme helpers | 46 | |
| 9917623619 | Competitive Inhibition | Bind to the active site of an enzyme, competing with the substrate | 47 | |
| 9917623620 | Noncompetitive Inhibition | Bind to another part of an enzyme, causing the enzyme to change shape and making the active site less effective | 48 | |
| 9917623621 | Allosteric Regulation | May either inhibit or stimulate activity, interaction in a site away from the active site which activates or deactivates a protein | 49 |
