Microbiology test two – Flashcards
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Six most common elements |
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CHONPS, Carbon hydrogen oxygen nitrogent phosphorus and sulfur |
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definition of catabolism |
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breaking down of complex molecules to release energy |
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Definition of Anabolism |
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is the set of metabolic pathways that construct molecules from smaller units. |
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metabolism |
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is comprised of both anabolism and catabolism |
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Anabolic cell growth is |
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turning simple compounds into complex by anabolic processes |
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Anabolic cell growth is |
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turning simple compounds into complex by anabolic processes |
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Energy used during anabolic process |
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ATP |
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Thermodynamics |
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study of energy by the calorie |
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Calorie |
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heat needed to raise on ml of H2O 1 degree celcius |
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kilocalorie |
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temp needed to raise 1000 ml of water one degree celcius |
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Two laws of thermodynamics |
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Energy cannot be created or destroyed but changes forms. energy goes from more concentrated to less concentrated by ways of entropy. |
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1st law of thermodynamics |
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energy cannot be created or destroyed but changes forms. |
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second law of thermodynamics |
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energy goes from more concentrated to less concentrated |
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exergonic reaction |
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reaction that releases energy spontaneous reaction |
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catalyzed |
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reducing activation energy |
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catalyzation in biological systems is |
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enzymes |
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ribosomes are |
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RNA enzymes |
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Metabolism deals with |
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enzymes by speeding up reactions |
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co-enzyme |
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are organic molecules that are required by certain enzymes to carry out catalysis. They bind to the active site of the enzyme and participate in catalysis |
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co factors |
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substance that needs to be present in addition to an enzyme for a certain reaction to take place. |
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non-competitive inhibitor |
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binds to allosteric site and changes shape of active site |
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factors controlling enzymes |
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substrate concentration, heat, ph, salt concentrations, heavy metals |
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temperature that enzymes work and work the best |
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37 degrees centigrade and 40 degrees centigrade |
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Competitive inhibitor |
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binds to active site and will not let the real substrate bind ex penicillin and peptidoglycan cell wall |
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v max of enzyme activity |
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maximum velocity or rate of reaction due to enzyme activity |
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proteins structure composed of |
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primary structure of petide bonds of amino acids, secondary structure of pleated sheet helical structure held by hydrogen bonds, tertiary structure give look of 3D view shape, quaternary structure consist of sub units for a 2 subunit protein |
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Active site of proteins with enzymes will on have this type of fit |
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complimentry fit |
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Hydrogen bonding is broken by |
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heat, salt, ph,substrates and heavy metals such as lead and mercury |
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Biological pathways allow enzymes to work together in |
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chains, substrate 1 to enzyme 1 to substrate 2 to enzyme 2 |
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Feedback inhibition |
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enzyme product is materials for enzyme 2 |
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last enzyme can effect first enzyme this way |
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the last enzyme can turn of first enzyme by making an allosteric enzyme that allows substrate to be used somewhere else |
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oxidation |
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oxidising material by a molecule losing an electron and losing hydrogen |
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Benefit to oxidation reaction in microbiology |
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electron lost is gained by another molecule |
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Reduction reaction |
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picking up of an electron and hydrogen and called redox reaction |
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Energy from oxidation reaction will get stored as |
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high energy molecule ATP contains adinine and ribose |
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heterotrophs |
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oxidase organic compounds of fats, proteins, sugars |
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lithotroph |
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oxidise reduce forms of inorganic compounds for carbon such as iron oxidizing bacteria sulfure bacteria |
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photoautotroph |
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convert light energy into chemical energy and use co2 as their carbon source |
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fermentation |
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partial oxidation of organic compout with final electron acceptor being another organic compound |
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steps to fermentation |
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ATP by production of glycolysis is split into 2 3 carbon chains to make 2 atp, its transfered to nad+ and reduced to NADH then is oxidised giving up H+ to pyruvate. THis is energy for lactic acid bacteria and yeast |
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glycolysis ? |
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Glucose phosphoralates by addition of phosphate and HExokinase adds phosphate to Po4 molecule. |
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atpases |
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will phosphoralate ADP and Make ATP and spin at a fast rate with the flow of hydrogen ions from outside to inside |
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glycolysis step 1 |
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1. addition of two phosphates to the 6 carbon molecule at the expense of two ATP- producing two ADP and creating 6 carbon sugar diphosphate. |
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glycolysis step 2 |
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The six carbon molecule with two phosphates is split into two three carbon molecule in a series of steps to pyruvate. The electrons are transferred to coenzyme NAD+ to form NADH and ATP is formed with 4 molecules of ATP formed. under aerobic conditions the pyruvate goes on to make more ATP and anaerobic to form lactic acid |
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common fermentation products are |
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ethanol and lactic acid. |
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glycolysis is |
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is a catabolic process in which a glucose molecule containing 6 carbons is split into 2 pyruvate molecules( 3 carbon molecule), Electron transfer from phosphate gives the coenyme Nad+ to turn it to NADH, during fermentation NAD+ is generated by the NADH giving up the electron and H+ to pyruvate to form the fermentation product. |
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lactic acid bacteria |
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streptococcus, lactobacillus |
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yeast(ethanol) bacteria |
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sacchromyces. |
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aerobic respiration |
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complete oxidation of glucose to CO2 and H20 and final electron acceptor is 02 |
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Glycolysis yields This |
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2 pyruvate(3 carbon chains) 2 Atp and 2 NADH |
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Kreb cycle yields |
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2 ATP |
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Kreb cycle |
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A co2 and NADH is giving off from conversion of Pyruvate to Acetyl-COA. 4 Carbon molecule is starting material and binds with acetylcoa creating a six carbon molecule with COA carrier molecule given off. Now CO2 is given off creating a 5 carbon molecule and a electron is given off to creat NADH. Next second decarboxylation occurs with CO2 and NADH given off with A molecule of ATP and 4 carbon molecule is formed. THe four carbon molecule is further oxidising hydrogens to give off NADH AND FADH2. |
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How many cycles must kreb cycle perform to yield 4 ATP? why |
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The kreb cycle must complete two rotations because the glucose molecule is breaking down two pyruvate and can only break down one molecule at a time making it have to cycle twice producing 4 atp |
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Properies of enzymes- structure |
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most are proteins, they have a tertiary structure thatthat allows for the presence of an active site that binds substrates and possibly co-enzymes (by lock and key) - |
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enzymes binding structure results in |
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enzyme-substrate complex, it reduces the activation energy of a reaction and alllow the reaction to occur very fast. Then releasing changed substrates which are now called products |
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Enzymes are reused Y or N? |
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YES!! |
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Enzyme specificity |
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specific as the reactions they perform and the substrates they will bind at the active site. |
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Can enzyme reactions reverse? |
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if there is not much difference between the energy of the substrates compared to the energy of the products energy difference is not much. |
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enzyme names end in |
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"ASE", protease example |
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co-enzymes |
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A nonprotein and if it is organic then it is a loosely-bound cofactors termed coenzyme. Coenzymes are relatively small molecules compared to the protein part of the enzyme. The coenzymes make up a part of the active site, since without the coenzyme, the enzyme will not function. example coenzyme A (CoA) usually the electron acceptor |
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co-factor |
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A cofactor is a non-protein chemical compound that is bound (either tightly or loosely) to a protein and is required for the protein's biological activity. flavin or heme are example |
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Decarboxylase involved in |
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Kreb cycle enzymes catalyze the decarboxylation of amino acids, beta-keto acids and alpha-keto acids[1]. for example Pyruvate decarboxylase catalyzes the decarboxylation of Pyruvate |
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dehydrogenase |
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is an enzyme that oxidizes a substrate by transferring one or more hydrides (H−) to an acceptor, usually NAD+/NADP+ or a flavin coenzyme such as FAD or FMN. |
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kinase |
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type of enzyme that transfers phosphate groups from high-energy donor molecules, such as ATP, to specific substrates. The process is referred to as phosphorylation. |
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fermentation atp net gain |
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2 ATP |
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NAD+ regenerated in fermentation by |
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The NADH giving up the electron and H+ to pyruvate to form the fermentation product. |
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ATP formed in Aerobic respiration is |
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formed by oxidative phosphorlation by glycolysis, krebs cycle, and ETS |
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Produced during kreb cycle |
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2 NADH FADH2 |
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role of oxygen in electron transport chain |
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o2 is the final electron accept to form H2O as the electrons travel through the electron chain protons are pumped across the cell membrane. |
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ATPase |
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catalyzes the formation of ATP by combining(phosphorylating) ADP(adenosine diphosphate) with inorganic phosphate ions to give ATP |
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glycolysis is found where |
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cytoplasm |
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electron transport chain is found where |
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Cell membrane |
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Glycolysis and kreb cycle is found in |
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cytoplasm |
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eukaryotes have kreb cycle in |
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mitochondria |
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light reaction needs |
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light |
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dark reaction can occur |
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w/ or w/o light at anytime |
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oxygenic photosynthesis |
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non-cyclic phosporalation with oxygen produced. |
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algea and cyanobacteria are able to carry this out |
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oxygenic photosynthesis |
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Nostoc |
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rod shape organism in chain, hetercyst and fix nitrogen. and oxygen we breathe first strated from these bacteria |
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photosystem |
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proton pumpes through membrane and electron actually goes back to the photosystem making it a cyclic system |
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Organism grows faster in fermentation or aerobic respiration |
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Aerobic respiration is better due to energy produced of 34 atp produced compared to 2 atp |
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difference between aerobic respiration and anearobic respiration |
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Aerobic respiration is the complete oxidation of glucose and final exctron acceptor is 02, 34 atp compared to 2 in fermenation. fermentation is partial oxydation of glucose with final electron acceptor being another organism. products of anearobic respiration are ethanol and lactic acid. they both share glycolysis |
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chemoautorophic bacteria |
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inorganic energy sources. Most are bacteria or archaea that live in hostile environments such as deep sea vents |
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chemoautotrophic bacteria |
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gain energ by oxidizing inorganic compounds. elements are Fe2, Sulfur, H2S. |
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sulfur-oxidizing bacteria |
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important in symbiotic relationship the surlfure-oxidizing bacteria are found inisde and the worms bring h2s and o2 to provide energy for the worm |
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oxygenic photosynthesis bacteria |
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cyanobacteria |
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anoxygenic photosynthesis bacteria |
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purple bacteria, rhodosprillum, chormatum |
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light reaction of photosynthesis produces |
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Oxygen and Atp |
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dark reactions need |
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Require ATP, NADPH, |
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dark reactions produce |
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glucose by calvin cycle |
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Dark reaction consist of |
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Carbon Fixation, Reduction reactions, and ribulose 1,5-diphosphate (RuDP) regeneration |
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Fred griffith |
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transforming principle, which is today known to be DNA, |
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fred griffith |
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The smooth strain (S strain) had a polysaccharide capsule and was virulent when injected, causing pneumonia and killing mice in a day or two. The capsule is a slimy layer on the cells' surface that allows the bacteria to resist the human immune system. The rough strain (R strain) did not cause pneumonia when injected into mice (it was avirulent), since it lacked a capsule. When the virulent S strain was heated to kill it, and then injected into mice, it produced no ill effects. However, when dead S strain mixed with live R strain was injected into the mouse, the R/S mouse died. |
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Avery,mcleod, mcarty 1944 |
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dead s. pneunomae break it apart by lysis Avery and his colleagues showed that DNA was the key component of Griffith's experiment, in which mice are injected with dead bacteria of one strain and live bacteria of another, and develop an infection of the dead strain's type. |
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hershey chase |
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use of bacteriophage In a first experiment, they labeled the DNA of phages with radioactive Phosphorus-32 (the element phosphorus is present in DNA but not present in any of the 20 amino acids from which proteins are made). They allowed the phages to infect E. coli, then removed the protein shells from the infected cells with a blender and separated the cells and viral coats by using a centrifuge. They found that the radioactive tracer was visible only in the pellet of bacterial cells and not in the supernatant containing the protein shells. |
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DNA is |
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helical shaped and comped of deoxyribose sugar as strands and phosphate bons that keep these together. |
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semiconservative dna means |
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Semiconservative replication would produce two copies that each contained one of the original strands and two new strands. |
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Dna polymerase bind at this site |
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to DNA at origin site. |
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to replicate DNA |
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Dna polymerase bind to dna at origin site, dna molecule fits right into the grooves becasue of its shape and hydrogen bonds break, strands are kept seperated by use of single strand binding proteins, Dna helicase(gyrase) unwind DNA ahead of Dna polymerase to get rid of tosional tension, Dna polmerase(primase) intitial start dna replication |
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Single strand binding proteins |
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come into play by keeping strands seperated |
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DNA helicase(gyrase) |
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unwind DNA ahead of Dna polymerase, actually cuts and flips dna and put its back together so dna is in straight line |
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What nucleotide bases are easiest to replicate |
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Origins tend to be "AT-rich" (rich in adenine and thymine bases) to assist this process, because A-T base pairs have two hydrogen bonds (rather than the three formed in a C-G pair)—strands rich in these nucleotides are generally easier to separate due to the few=flexibilty/many=durability relationship found in hydrogen bonding. |
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DNA Polymerase |
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"reads" an intact DNA strand as a template and uses it to synthesize the new strand. The newly-polymerized molecule is complementary to the template strand and identical to the template's original partner strand. Codes from a 5' end to 3' on leading strand |
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Dna replicates at this end |
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DNA polymerase can add free nucleotides to only the 3’ end of the newly-forming strand. |
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Laggin strand |
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gaps where dna is not copied 5' to 3' |
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how Laggins strand is copied |
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Also needs to have 5' to 3' and Rna polymerase lays down RNA primer then DNA polymerase comes in to lay down dna from the RNA fragments. Then DNA ligase links the fragments together |
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Leading strand |
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Leading strand of continues replication 5' to 3' direction |
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DNA ligase |
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connect Po4 to hydroxyl when runs into new strand after exonuclease replaces RNA w/ DNA then 5' and 3' join together |
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exonuclease |
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replaces RNA w/ DNA |
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Eukaryotic things have this to make DNA replication run faster |
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multiple sites of Origin to allow DNA to be copied faster |
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Every replication the chromosomes |
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get shorter |
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Telomerase |
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repeats ("TTAGGG" in all vertebrates) to the 3' end of DNA strands in the telomere regions, which are found at the ends of eukaryotic chromosomes. adds telomere each time |
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telomere |
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A telomere is a region of repetitive DNA at the end of a chromosome, which protects the end of the chromosome from destruction. |
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cells that constantly divide |
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sperm, white blood cells, cancer cells |
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Proof reading dna |
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Makes a mistake and moves about 1,000 bases a second, WHen a mistake is made DNA polymerase goes backward to fix it. |
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Direction exonuclease activity runs and why |
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3'to 5' to elimnate bases until it feels right and goes forward again |
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transcription |
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copying |
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messenger rna |
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working copies of a gene |
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Gene expression / protein syn |
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dna, transcrption, messenger rna, translation, to protein |
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how to write out gene name |
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Italisized or underlines with 3 letter designation |
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Gene |
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sequence of DNA that codes for a protein or trait |
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DNA |
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double stranded made of deoxyribose |
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RNA |
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single stranded, nucliotide of ribose, No T's in RNA and replaced with U's, functional working copy |
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RNA polymerase |
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makes transcription enzyme and looks for start of the gene |
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start of the gene |
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promotor region |
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Single strand binding proteins |
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Protein that binds to single-stranded DNA usually near the replication fork to stabilize the single strands. |
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sense strand |
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dna of trait needed |
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Summary of Dna Replication at the fork |
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enzymes unwind the parental double helix, proteins stabilize the unwound parental DNA, the leading strand is ynthesized continously by dna polymerase, the laggin strand is synthesized discountinously. and rna polymerase synthesizes sshort rna primer, which is then extended by dna polymerase and dna polymerase digest RNA primer and replace it with dna, dna ligase joins the discontinous fragments of laggin strand. |
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promotors are |
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full of a's and t's and are promotor sequence that are 10 sequence from start and 35 from the start. |
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Sigma factors |
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factors that enable rna polymerase to bind to specific promotor sites |
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transcription factors |
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transcription factor is a protein that binds DNA at specific sites where it can regulate transcription. |
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cimplementary base pairing between sense strand of dna and resulting messenger RNA |
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3' ATGCAT to 5' UACGUT |
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Primase |
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adds a short piece of RNA called an RNA primer at which DNA can synthesize the 3 prime end |
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Rnase |
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removes RNA primers and leaves a gap that is filled by DNA polymerase |
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Three processes in transcrption |
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Initiation, Elongation, termination |
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intiation |
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The RNA polymerase binds to promotr site and replicates at the 3' end |
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template strand |
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serves as one copy for transcription and RNA has a complimentary strand to this |
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elongation |
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forms a bubble and rna polymerase adds bases to 3' prime end of growin rna transcript and continues until it hits a terminator site |
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terminator site |
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at this site rna polymerase and new rna transcript are released from dna, and can occur for self termination, and enzyme termination |
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self termination |
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the rna sequence transcribe at the terminator makes it bind to hydrogens to itself making a loop structure pushes rna polymerase of dna |
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enzyme dependant determination |
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a termination protein enzyme binds to terminator releasing rna polymerase |
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translation |
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uses a mRNA to synthesize a protein, ribosomes read along a mRNA reading the genetic code to aminoa acid sequence in the protein and in bacteria can happen before transcription is completed |
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Codons |
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64 three letter words and genetic code. and 61 of 64 code for genetic material and 3 of 64 code to stop translation |
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start codon |
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shows where to start the translation to the tRNA |
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Start codon needs |
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Anti codon on each tRNA is complimentary to the Codon on the mRNA in translation |
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tRNA |
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goes from sequence to sequence to to create the polypeptide site, |
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A or amino acid site of tRNA |
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amino acid site hold new tRNA with new amino acid attached |
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E site allows |
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used tRNA to exit from ribosome |
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Stop codon |
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a protein called release factor binds in a site and new rna and polypetide are released, the ribosomes are recycled to continue the process |
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operon in bacteria |
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promotor, operater, structural genes |
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structural genes |
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transcribed into mRNA |
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operons need |
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inducer while repressible operons are always to be able to transcribe |
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control region |
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promotor, operator region |
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lac operon |
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is an induced operon meaning genes are not really transcribe but induced to produce the proteins of catabolism when present in the cell |
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lactose produces allolose that |
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blocks the repressor and alows for transcription of lactose |
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regulatory gene produces repressor until |
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the lactos or co repressor is present in the cell letting transcription take place |
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repressor proteins |
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create a block on the operator preventing Rna polymerase from going |
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inducer and example |
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inducer inactivates the repressor and example for lactose is allolactose |
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bacteria transcription occurs |
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cytoplasm and transcription and translation can occur at the same time |
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In eukaryotes |
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transcription occurs in Nucleas and messenger rna leaves through nuclear pores |
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Rna in eukaryotes has sequences that |
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code for nothing to interrupt gene sequence. |
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removal of lactos from around cell |
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the repressor stops RNA transcrption |
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Repression |
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the Rna polymerase constantly produces its gene of tryptophan. the regulatory gene produces repressors that are inactive until too many tryptophan are produce that induce the repressor to bind to the operator stoping RNA polymerase |
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induction |
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uses for ex. allolase as an inducer to the lac operon because the repressor is always attached to the operator region. When the lactose is in the cell its allolase inducer binds to the repressor making a substance to break down lactose. The lactose must be present to knock off the repressor |
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framshift mutations |
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basesubstitution mutations |
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when a single nucliotide substitutes for another. nonuse mutation, silent mutation, missuse mutation |
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missuse mutation |
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single amino acid substitution can be harmful, beneficial, or nuetral |
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silent mutation |
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just a change in base pairing and nothing is affected |
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nonsense mutation |
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changes codons to make a stop codon which causes early termination of the protein and can be very harmful |
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framshift mutation |
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nucliotides are inserted into or removed from dna sequence, lead to non functional proteins |
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framshift insertion |
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one or more bases added to dna sequence and cause non functioning protein |
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framshift deletion |
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one or bases are removed from dna squence cause non functioning protein |
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chemical mutations |
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mutation are called mutagens. Most of them are also carcinogens. |
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uv light mutations are by |
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UV light can induce adjacent thymine bases in a DNA strand to pair with each other, as a bulky dimer. |
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radation mutagens |
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ionizing radiation xrays and gamma rays cause molecules to lose electrons becoming free radicles and highly radioactive to combine to bases on dna and result in errors and can react to phosphate backbone causeing breaks. |
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non ionizing radiation |
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cause thyamine dymers to attach to one another and prevent cell from copying dna |
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chemical mutagens |
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nucliocide analogs, different base pairings and come incorporating into dna and cause dna to not be able to be copied later, nitrous acid can cause adinine bases to pair to cyctocine bases, cause small insertions or small deletions, acridine, benzopyrine = from soot and smoke |
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biological mutation |
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mutation of DNA during replication |
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horizontal gene transfer |
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conjugation, transformation, transduction |
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competent bacteria |
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are able to pick up dna from their environment and are stapholococcus pnumonia and ecoli(through lab work) |
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transformation |
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bacteria is able to pick up dna from its environment. rough live and dead smooth come together to kill the mouse showing they incorporate from environment. |
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transduction |
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a virus(bacteriophage) injects dna into the bacteria to replicate new viruses and the bacteria is transferred into the new virus being produced this virus then goes and infects bacteria and its dna is incorporated into the bacterias dna causing recombination. |
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control of gene expression |
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negative control = repression |
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A or amino acid site |
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holds new tRNA with amino acid attached |
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p or polypeptide site |
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hold previous tRNA with growing polypeptide attached |
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avery |
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Avery and his colleagues suggest that DNA, rather than protein as widely believed at the time, may be the hereditary material of bacteria, and could be analogous to genes and/or viruses in higher organisms |