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| 7169189454 | Protein Structure | Proteins are formed by polypeptides. Polypeptides are formed by linked amino acids | 0 | |
| 7169193343 | Amino Acids | The building blocks of proteins. They can be characterized by their reactivity to of their R group as nonploar, polar, acidic, basic, and aromatic. | 1 | |
| 7169197374 | Phe | UUU and UUC | 2 | |
| 7169198714 | Lue | UUA, UUG, CUU, CUC, CUA, and CUG | 3 | |
| 7169199839 | Ser | UCU, UCC, UCA, and UCG;AGU and AGC | 4 | |
| 7169200842 | Tyr | UAU and UAC | 5 | |
| 7169201235 | Stop | UAA, UAG, UGA | 6 | |
| 7169201748 | Cys | UGU and UGC | 7 | |
| 7169202291 | Trp | UGG | 8 | |
| 7169202582 | Pro | CCU, CCC, CCA, and CCG | 9 | |
| 7169207963 | His | CAU and CAC | 10 | |
| 7169208494 | Gln | CAA and CAG | 11 | |
| 7169208849 | Arg | CGU, CGC, CGA, and CGG; AGA and AGG | 12 | |
| 7169209676 | Ile | AUU, AUC, and AUA | 13 | |
| 7169211154 | Met | AUG | 14 | |
| 7169211478 | Thr | ACU, ACC, ACA, and ACG | 15 | |
| 7169212296 | Asn | AAU and AAC | 16 | |
| 7169213031 | Lys | AAA and AAG | 17 | |
| 7169213562 | Val | GUU, GUA, GUA, and GUG | 18 | |
| 7169220862 | Ala | GCU, GUC, GUA, and GUG | 19 | |
| 7169222698 | Asp | GAU and GAC | 20 | |
| 7169224282 | Glu | GAA and GAG | 21 | |
| 7169224498 | Gly | GGU, GGC, GGA, and GGG | 22 | |
| 7169228663 | Primary protein structure | sequence of a chain of amino acids |  | 23 |
| 7169229909 | Secondary protein structure | Hydrogen bonding of the polypeptide back bone causes the amino acids to fold into repeating patterns |  | 24 |
| 7169235496 | Tertiary protein structure | Thre dimensional folding pattern of a protein due to side chain interactions | 25 | |
| 7169237120 | Quaternary protein structure | protein consisting of more than one amino acid chain |  | 26 |
| 7169244780 | Non Enzymatic Protein Function | They function as antibodies, apart of the adaptive immune response; they can also be cell surface receptors | 27 | |
| 7169257793 | Enzymes | Protein folded into a specific 3-Dimensional shape to act as a catalysts | 28 | |
| 7169259521 | Active Sites | Area in the protein that performs catalysis with the reaction's substrates | 29 | |
| 7169264196 | Catalysis | A biochemical reaction facilitated by an enzyme for conversion of reactants into products | 30 | |
| 7169265871 | Catalysts | A material that increases the rate of a reaction by lowering the activation energy |  | 31 |
| 7169271211 | Active Site Model (Lock and Key) | A theory suggesting the enzymes and substates are a perfect fit for each other. |  | 32 |
| 7169273976 | Induced Fit Model | The substrate and the binding site differ slightly and binding induces conformational change |  | 33 |
| 7169278803 | Feedback Inhibition | When an intermidiate or end product inhibits one of the other enzymes that proceed it. This prevents wastful over production of the product. | 34 | |
| 7169282917 | Covalent Modification | Addition or removal of different groups in order to active or inactivate an enzyme | 35 | |
| 7169285103 | Proteolytic Cleavage | This is for enzymes such as zymogen which are synthesized in an inactive state and must be cleaved into activation by a protease | 36 | |
| 7169298772 | Constitutive | The enzyme subunit is removed | 37 | |
| 7169301242 | Allosteric Regulation | Modification of the active-site activity by interaction of molecules with other specific sites | 38 | |
| 7169303602 | Allosteric Sites | Where the interaction with other molecules takes place | 39 | |
| 7169305329 | Competitive | Inhibitors can compete for the binding site and out compete the substrate if the concentration is high enough | 40 | |
| 7169310972 | Noncompetitive Inhibitors | Binds at the allosteric sit, not the active site, and it won't budge even if the substrate is in high concentration | 41 | |
| 7169314633 | Uncompetitive Inhibitors | Can only bind to the enzyme-substrate complex | 42 | |
| 7169316432 | Mixed-type inhibitors | Can bind to the unoccupied enzyme or the enzyme-substrate complex | 43 | |
| 7169322085 | Michaelis-Menten | Rate of metabolism of a drug at or near saturation |  | 44 |
| 7169323167 | Cooperactivity | The binding of one subunit to an enzyme allosterically increases the affinity for the next subunits or substrate, leading to a sigmoidal kinetic graph | 45 | |
| 7169340461 | Bioenergentics | The production and utilization of energy in a biological system that all boils down to reduction and oxidation reaction | 46 | |
| 7169344090 | Monosaccharide | A single carbohydrate molecule. The carbons in monosaccharides are numbered from the carbon at the most oxidized end of the molecule. They can exist as a chain or a ring |  | 47 |
| 7169358782 | Disaccharide | Two disaccharides bind together though a dehydration reaction called glycosidic linkage | 48 | |
| 7169365331 | Oligosaccharide, Polysaccharides | multiple disaccharides conected through glycosidic bonds | 49 | |
| 7196091838 | Glycolysis | Occurs in the cell cytoplasm converting 1 Glucose into 26-28 ATP |  | 50 |
| 7196103841 | Fermentation | The process of converting pyruvate into either ethanol or lactose |  | 51 |
| 7198933470 | Glycogenolysis | The break down of glucose polymer, glycogen, this is done so individual glucose ,molecules can be used for cellular respiration | 52 | |
| 7198947919 | Gluconeogenesis | The synthesis of glucose when the molecule diet wise is unavailable | 53 | |
| 7198984596 | Pentose Phosate | Takes glucose-6-phosphate from glycolysis in order to mak ribose-5-phosphate. This compound is used to synthesis nucleotides | 54 | |
| 7199014139 | Citric Acid Cycle (Kreb's Cycle) | A collection of reactions that takes the 2 carbon acetyl unit from CoA, combines it with oxaloacetate, and release 2 CO2, generating 2 NADH and FADH2. |  | 55 |
| 7199044968 | Oxidative Phosphorylation | Oxidation of high-energy electron carriers NADH and FADH2 | 56 |
