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micro module 2
chaps 8, 9 , 10 Talaro
| Question | Answer |
|---|---|
| def of carbohydrate | this chemical class resemles combos of carbon and water |
| def amino acids ; how many | building blocks of proteins they have a baisc skeleton consisting of carbon linked to an amino group and carboxyl group and hydrogen atom; 20 |
| def of lipids | fat an optional term for a variety of substances that are not soluble in polar solvents (ei Water) but dissolve in nonpolar substnaces |
| def of proteins; how many amino acids do they contrina | building blocks of proteins are amino acids they are what give structure behavior and unique qualities to living things; at least 50 |
| def nitrogen base ; what arethe 2 fomrs ; what are the 2 purines; what are the 2 pyrimidines | nitrogen subunit of nucleotide; purines and pyrimidines ; Adenine (A) and guanine(G); Thymine (T) and cytosine (C) |
| def covalent bond | they form between atoms with valences that suit them to sharing electrons rathern than donating or receiving them |
| def oxidation | any reaction that causes an atom to lose electrons |
| def hydrogen bond; how is this represented in drawing | this bond does not involve sharing, losing or gaining electrons but is a weak electrostatic force that forms between hydrogen covalently bonded to one molecule and an oxygen or nitrogen atom ; with dotted line |
| def inorganic compund | |
| def monosacharide | a simple polyhydroxy aldehyde or ketone molecule containing 3-7 carbons |
| def phospholipid; is it hydrophobic or hydrophilic | structural component of cell membranes they contrina only 2 fatty acids attached to the glycerol and the third glycerol binding dite holds the phosphate group; both are located on it |
| def peptide | a molecule composed of short chains of amino acids |
| def polar; what is polarirty ; def nonpolar | a molecule with unequal distribution of charges and shows polarirty; the molecule has a negative and positive pole; electrons are shared equally between 2 atoms and the molecule in neutral |
| def reactant; what is the result of a chemical reaction called | the chemical substances that start a reaction and that are charged by the raction; products |
| def disaccharide | a combo of 2 monosaccharides |
| def hydrolysis reaction | a water molecule is required to break the bond between 2 glucose molecules |
| def peptide bond | a covalent bond that forms between the amino group on one amino acid and the carboxyl group on another amino acid (these join amino acids ) |
| def enzyme | serve as teh catalusts for all chemical reactions in cells |
| def substrate | |
| def nucleotide ; what are the 2 smaller units | DNA and RNA are these polymer of repeating units; nitrogen base, sugar and phosphate |
| def electrolyte | |
| def reversible reaction | the reactants and products can be converted back and forth this depends on the proportions of the compounds |
| def functional group | |
| def synthetic reaction | the reactants bond together that produces an entirely nre molecule |
| def cation | positively charged ions |
| def anion | negatively charged ions |
| def ion | they are unattached charged particles from a broken down ionic bond |
| def triglyceride | storage lipidscomposed of single molecules of glycerol bound by 3 fatty acids |
| def cholesterol | a sterol it is complec tinged compound found in cell membranes and animal hormones it reinforces the cell membrane in animal cells |
| def polypeptide | contains an unspecified number of amino acids but usually more than 20 and is often a smaller subunit of a protein |
| def deoxyribonucleic acid | DNA, a nucleic acid; mster computer of all cells contains codes of genetic info for instructions of each organisms heredity |
| def anedosine triphosphate ; aka | a nucleotide contrasining adenine ribose and 3 phosphate rather than one, it releaes and stores energy for chemical reactions; ATP |
| def polysaccaride | a polymer of five or more monosaccarides bound in linear or branched chain pattern |
| def fatty acid | long chain unbranched hydrocarbon molecules with a carboxyl group at one end that is free to bind the the glycerol |
| def disulfide bond | |
| def oxidation-reduction | this substance can cause oxidation by taking electrons or it can be a substance that causes reductions by giving away electrons |
| def dehydration synthesis | in order to form a carb bond one carbon gives up its OH group and the aotehr loses H from its OH group. Water is the product of this reaction |
| def monomer | all macromolecules except lipids are formed by polymerization a process in which repeating subunits termed polymers |
| Atomic Structure: def atom; what are the particles in an atom; def protons; def neutrons; def of electrons; what forms nucleus of an atom | all matter in the universe composed of this simple form of matter; protons, neutrons and electrons; positively charged particles; no charge; negatively charged; protons and neutrons |
| def ionic bond | electrons are transferred completely from one atom to another and are not shared |
| atomic structure: what orbits the nucleus in energy shells; def of atomic number ; def of mass number; how many electroms are in 1st shell; how many electrons can be in seconds shell; | electrons; this is the number of protons; the number of ptrons + neutrons; 2; 8 |
| atomic structure carbon- how many shells does it have; what is atomic number ; what is atomic mass; how many electrons; | 2; 6; 12; 6 |
| atomic structure hydrogen: atomic number ; atomic mass; how many protons; how many electrons | 1; 1; 1; 1 |
| atomic structure oxygeon: atomic number; atomic mass; how many protons; how many neutrons; | 8; 16; 8; 8 |
| atomic structure nitrogen: atomic number; atomic mass; how many protons; how many neutrons; | 7; 14; 7; 7 |
| hydrogen: how is the molecule formed; each hydrogen molecule only has __ in outer shell; is this covalent of ionic bonding | when 2 hydrogen atoms share their electrons and form a single bond; 1 so they need one to make outer shell full; covalent |
| oxygen: how do two oxygen molecules share to form oxygen; is this covalent or ionic bonding | they share two molcules from each orbital to make O2; covalent |
| hydregen bonding: more extensive hydrogen bondign is responsible for what | the structure and stability of proteins and nucleic acids |
| def hydrolysis: catabolic reactions involving energy transactions are eually active and require ___; hydrolysis reaction got its name why; def | their own enzymes; they breaking of bonds usually requires the input of water; digestion of large substrates requires enzymes to break them down into smaller molecules so they can be used |
| def of oxidized; def oxidation | these are compounds that lose electrons; the loss of electrons |
| def of reduced; reduction | these are compounds that receive electrons; the gain of electrons |
| def of redox reaction; these reactions occur in ___; | this is oxidation-reduction are common in the cell and indispersable to energy transactions; pairs |
| def of labile | chemically unstable enzymes |
| def of denaturation; this destruction causes what; these nonfunctional enzymes block what | rpocess by which the weak bonds that collectively maintain that native shape of the apoenzyme are broekn; extrem distortion of enzymes shape and prevents the substrate from attaching to the active site ; metabolic reactions and can lead to cell death |
| def of competitive inhibitions: what is it; | a form of inhibition done by bacteria that they use a mimic substate for enzyme so enzyme will be occupied with fake substrate instead if reall one |
| def of negative feedback | |
| def of endergonic; | this cellular reaction is driven forward with the addition of energy |
| def of exergonic; why is this energy considered "free energy"; | a cellular reaction that releases energy as it goes forward; b/c it is available to do work |
| def of phosphorylate | this is the addition of phosphate to a substrate |
| def of dephosphorylate | is the removal of a phosphate from a substrate |
| def of dehydrogenation | removal of a hydrogen |
| def of decarboxylation | removal of carbon dioxide from a substrate |
| def of catabolism; def anabolism; anabolism is aka | larger molecules are degraded or broken down into smaller molecules with release of energy; smaller molecules build larger ones and results in the formation of cell structures it uses energy; biosynthesis |
| def metabolism; what are the 2 categories of it | change pertains to all chemical and physical workings of the cell; catabolism and anabolism |
| enzymes: what are they; they are an example of ____; def of catalysts; does an enzyme create a reaction; | proteins; catalyst; chemicals that increase the rate of a chemical reaction without becoming part of the products or being consumed in the reaction; no; |
| enzymes: are the used up or perminently changed by a reaction; can they be recycled; what are they greatly effected by; | no; yes; temp and pH; |
| enzymes: in chemical reaction reactants are converted to what; enrgy is needed to initiate every such reaction and this limits its __; this resistance to a reaction is measurable by what | products; rate; energy of activation |
| enzymes: how is the initial resistance overcome in lab; | increaseing thermal energy (heat) to increase molecular velocity, increasing concentration of reactants to increase rate of collisions, adding a catalyst |
| enzymes: the reactant molecules are aka; are they larger or smaller than substrates; how is shape unique; do enzymes become part of the product because they bind to the substrate; how is the speed of enzyme measured | substrates; larger; that it has pocket that fits only a particular substrate; no; by number of substrate molecules converted per enzyme per second |
| enzyme: what is promary structure of it; what are the 2 classifications; def of simple; | proteins; simple conjugated; only contrins protein; contains protein and nonprotein molecules; |
| enzymes: what is name for the pocket where subtrate binds; | the active site |
| enzymes: for reaction to take place what union must occur; this union is aka; what happens once enzyme-substrate complex is formed; | a temporary enzyme-substrate union in active site; lock and key fit; the appropriate reaction occurs on the substrate |
| enzymes: def of cofactor; def coenzymes; | meital ions (iron, copper, mag., etc) that activate enzymes and help brin active site and substrate close together and participates in chemical reaction; organic cofactors that remove a chemical group from substrate colecule |
| enzymes: how are they classified; | according to characheristics such as site of action, type of action and substrate |
| enzymes: in disease: what are exoenzymes; aka | pathogens secrete these the help them avoid host defenses or promote multiplication in tissues; endo toxins or virulence factors |
| enzymes: enzymes like to operate in what; def of labile | the natural habitat of cells environment; when enzymes are subject to change in normal conditions they become chemically unstable; |
| enzymes: regulation of metabolism is largely due to regulation of enzymes why; | b/c enzymes are critical to metabolic reactions; |
| enzymes and metabolic pathways- each step in the pathway is catabolized by what; enzymes set the rate of what; | an enzyme; the pathways progression; |
| controlling action of enzymes: how can bacteria inhibit enzyme activity called competitive inhibition; | it will supply a molecule that resembles the enzyme's nromal substrate and the mimic will occupy the enzymes active site preventing actual substrate from binding there; |
| controlling action of enzymes: def of regulatory/allosteric site | a form of inhibition where enzyme has 2 binding sites this site is that it provides a negative feedback system that can slow down enzymatic activity once a certain number of products is produces (this regulates) |
| enzymes synthesis: def of enzyme repression; def of enzyme induction; enzyme inductions is good why | a means to stop further synthesis of an enzyme somewhere along its pathway; enzymes are induced only when suitable substrates are present- the synthesis of an enzyme is induced by its substrate; prevents microbe from wasting energy |
| def of energy; name the forms of energy | the capacity to do work or to cause change; thermal, radiant, electrical, machanical, atomic, chemical energy |
| energy: where is thermal energy from; radient energy from; electrical energy from; machanical energy from; atomic energy from; chemical energy from; | molecular motion; visible light or other rays; flow of electrons; physical change in position; reactions in the nucleus; bonds of molecules |
| energy: how do cells manage it; why are exergonic and endergonic reactions coupled together; | in the form of chemical reactions that change molecules; the released energy from the exergonic reaction is then used by the endergonic reaction |
| energy: cells extract _____ in nutrient fuels and apply that energy to what | chemical energy; useful work in the cell |
| energy: during exergonic reactions what is pulled out of the atom; the removal of the electrons releases what; the harvested energy from the electrons is transferred to what molecule; ATP releases its energy for what reactions | electrons; this releases their ingerent energy; ATP; endergonic ones |
| ATP is constantly being ___, ___, ___ | made used and regenerated |
| ATP: how many parts are there;made of what; what is it classified as; ribose is what; | 3; adenine and ribose (5 carbon monosaccharide) and 3 phosphate groups; nucleic acid; 5 carbon monosaccharide |
| ATP: what happens when the bonds of the phasphate groups are broken; breaking the bonds between 2nd and 3rd phosphate groups yeilds what moleucle; | there is a release of free energy; ADP |
| Hydrolysis of ATP: this does what; ATP + ___ through a hydrolysis reaction uses what enzyme; To form ATP from ADP you need what; | frees the molecule; water; ATPase; adentazyne phasphate group PO4 plus energy |
| redox reactions: oxidation and reduction always occur __; ozidation is the loss of what;reduction is the gain of what; | simultaneously; electrons/ hydrogen atom; electrons/ hyfrogen atom |
| hydrogen atom: has how many protons; how many electrons | 1;1 |
| REDOX: way to remember this; what does leo says ger stand for; | LEO says GEr; less equals oxidation (loos of electrons_; gain equals reduction (gain of electrons) |
| redox: they always occur in pairs with an electron donor and electron ecceptor, what is the name for this pair; electron transfer is __ transfer | redox pair; energy |
| coenzymes: used to transport what; | hydrogen atoms to electron transport system; |
| coenzymes: nicotinamide adenine dinucleotide: what is abrev.; what is oxidized form; what is reduced form; it is reduced when it comes into contact with what; is it charged | NAD+; NAD+; NADH + H+; hydrogen atoms; yes |
| conenzymes: flavine adenine dinucleotide- what is abreviated name; is it charged; what is oxidized form; what is reduced form; reduced how; | FAD; no ; FAD; FADH2; it picks up 2 hydrogen atoms |
| phosphorylation: def; ADP + ___ +____ = ___ | process that adds an inorganic phosphate Pi to a substrate, converting it to ATP; phosphate (P) + energy = ATP; |
| def of hydrolysis; does this create a larger molecule or release of two smaller molecules | the addition of water; creates 2 smaller molecules |
| def of dehydration synthesis; does this create a larger molecule or release of two molecules | the removal of water; creates a larger molecule |
| dephosphorylation: def; give example | the removal of a phosphate; ATP hydrolysis (breaks down to ADP) |
| def of bioennergetics | the study of the mechanisms of cellular energy releases, including catabolic and anabolic routes |
| catabolism: what are the common paths used by many organisms | glycolysis, Krebs cycle, respiratory chain |
| cellular respiration in bacteria: def; def of anaerobic respiration; in anaerobic respiration what may some species use as final elctron ecceptors; what are three it involves; | a series of catabolic pathways leading to the formation of ATP; cell forms ATP w/o using free O2 as the final electron acceptor; nitrate, sulfate, CO2; glycolysis, Krebs cycle and electron transport system |
| cellular respiration in bacteria: def of fermentation; | cell uses glycolysis to form ATP and an organic molecule is the final electron acceptor; |
| cellular respiration in bacteria: aerobic respiration: def; | cell forms ATP while consuming free oxygen and oxygen in the final electron acceptor |
| cellular respiration in bacteria: what produces most ATP aerobic respiration, aneorbic respiration or fermentation | aerobic respiration |
| most common catabolic pathways: name the five | glycolysis, transition reactions, Krebs cycle, electron transport chain, fermentation |
| aerobic respiration (bacterial cell): glucose- what is the molecular formula; after aerobic respiration what does it yeild; the end products are energy rich ____ and energy poor __; | C6H12O6 + 602 +38 ADP + 38 Pi; 6CO2 + 6H2O + 38 ATP; energy rich ATP and energy-poor carbon dioxide |
| Aerobic respiration; glycolysis: def; how many steps are there; site where is takes place; reactions of glycolysis occur in how many parts; | this converts flucose through several steps into pyruvic acid; 9; cytosol; 2 |
| Aerobic respiration; glycolysis: what is first part of glycolysis called; def of endogonic; what is 2nd part of glycolysis called; def of exergonic | endogonic; uphil reactions energy is consumed; exergonic; downhill reactions and energy is released |
| Aerobic respiration; glycolysis: goal of it; | to release energy and to form ATP; |
| Aerobic respiration; glycolysis: 1st part- what molecule do you start with; how many carbons does glucose have in start of glycolysis; what is metabolic formula of glucose; what is hydrolyzed in beginning; | glucose; 6; C6H12O6; 2 ATP |
| Aerobic respiration; glycolysis: 1st part- when ATP is hydrolyzed what does that releases; what does glucose pick up from the product of hydrolysis; what molecule is formed from glucose picking up energy and inorganic phosphate; still 6 carbon | 2 ADP + 2 inorganic phosphate molecules (P)+ energy; the energy and the 2 inorganic phosphates; fructose-1, 6-disphosphate; yes |
| Aerobic respiration; glycolysis: 1st part- what is initial substrate; what 1st phosphorulated; when the 2 ATP are hydropyzed what kind of reaction is this and why; at end of 1st step how many carbon are there | glucose; glucose; endergonic reaction b/c substrate gets energy; still 6; |
| Aerobic respiration; glycolysis: 2nd part- what kind of reaction is this; what substrate do we start with; what is it borken down into; what are the names of the 2 three carbon molecules; | exergonic; fructose-1, 6-diphosphate and 6 carbons; 2 three carbon molecules; PGAL molecules (there are 2 of them); |
| Aerobic respiration; glycolysis: 2nd part- does each PGAL molecule go through same process; what first happens to PGAL; the 2 NAD+ are reduced to what; after it is phosphorulated it is then __; anough energy is being released to form 2 ADP molecules into | yes; it is phosphorulated; 2 NADH+ H+; oxidized; 2 ATP molecules |
| Aerobic respiration; glycolysis: 2nd part- what is the end product; how many carbons are in pyruvate; how many carbon total | 2 pyruvate 3 each; 6 |
| Aerobic respiration; glycolysis: end product summary- how many aTP produced; how many ATP consumed; How many ATP gained; how many NADH+ H+ gained; how many pyruvate gained; do we still have original carbon molecules | 4; 2; 2; 2; 2; yes |
| Aerobic respiration; glycolysis: end product summary- the 2 NADH + H+ formed are transported to what next; | the electron transport system; |
| Aerobic respiration; glycolysis: what two carbons of glucose have been fosphorulated, | the 1st and 6th; |
| Aerobic respiration: transition reaction prior to the krebs cycle: why does pyruvic acid enter the krebs cycle; | for processing and energy release; |
| Aerobic respiration; glycolysis: what is the next step after glycolysis in aerobic respiration; what is transition reaction; | for pyruvate to be dealt with in transition reaction; it prepares pyruvate to enter the Kreb's cycle as acetyl; |
| Aerobic respiration: transition reaction prior to the krebs cycle: where in cell does transition reaction take place; what is initial substrate; 2 pyruvate molecules each 3 carbons in length is de___ & ___; | cell membrane; the 2 pyryvate from the end product of glycolysis; decarboxylated and oxidized; |
| Aerobic respiration: transition reaction prior to the krebs cycle: in decorboxylation what is pulled off of the pyruvate; what happens in oxidation; so NAD+ is reduced to what; what is added to each pyruvate; what is end products; how many carbons in end | 2 CO2 molecules; 4 hydrogen atoms pulled off the 2 pyruvate; NADH + H+; coenzyme A; 2 acetyl-CoA; 2 each so 4 total (loss of 2) |
| Aerobic respiration: transition reaction prior to the krebs cycle: summary- so 2 NADH + H+ produce what; | 2 C02 molecules that are pulled off and that is waste and 2 Acetyl-CoA (these have a 2 carbon backbone a piece) |
| aerobic respiration: what is after transition reaction | krebs cycle |
| aerobic respiration: krebs cycle: what is the initial substrate that it starts with; how many carbons are in the acetyl-CoA; so how many original carbons from glucose do we have; | 2 Acetyl-CoA; 2 each so 4 total; 4; |
| aerobic respiration: krebs cycle: when the 2 acetyl-CoA molecules enter what does the 2-carbon acetyl group immediately bind with; the binding of these 2 form what; how many carbons does citric acid have | each of the 2 acetyl group bind to one 4-carbon oxaloacetate molecule; 2 citric acid molecules; 6; |
| aerobic respiration: krebs cycle: so when the 2 acetyle groups bind with the 4 carbon oxaloacetate molecules what is released fr om the acetyl group; where does krebs cycle take place; | the coenzyme A; along cell membrane; |
| aerobic respiration: krebs cycle: since there are 2 citrate at end of combo from acetyl and oxaloacettic how many carbons total with two added; how many carbons are the original from glucose; what is next step after citrate formation | 12 C; 4 (2 in each citrate molecule); decarboxilation of citrate |
| aerobic respiration: krebs cycle: when decarboxilation of the citrate occurs how many carbon molecules are lost; what happens when the the citrate is oxidized; so what happens to the NAD molecules | 4 carbon molecules from the citric acid; it gives of hydrogen atoms; they pick up 4 hydrogen atoms forming NADH+ H+ |
| aerobic respiration: krebs cycle: enough energy is released to form what; how are the 2 ATP formed; so after citrate is decarboxylated and oxidized what is formed; | 2 ATP molecules; with combo of ADP and inorganic phosphate; 2 succinate; |
| aerobic respiration: krebs cycle: how many carbons do teh 2 succinate have; why is succinate firther oxidized; what is the coenzyme used for succinate | 4 each so 8 total;b/c it contains some hydrogen atoms still; FAD |
| aerobic respiration: krebs cycle: how many FAD molecules are pick up 4 hydrogen atoms; when FAD picks up hydrogen atoms what does this form; what happens to the @ NAD+; what is the end result of the succinate; | 2; 2 FADh2; they are reduced as well; 2 oxaloacetate molecules; |
| aerobic respiration: krebs cycle: with the end result of 2 xoalocetate this can be used how; when is original glucose completely catabolized; | through the cycle over and over again; when succinate turms into oxaloacetate; |
| aerobic respiration: krebs cycle: remember all of these reactions are ___; | enzymatic reactions |
| aerobic respiration: krebs cycle: summary- how many CO@ molecules formed; what is waste; how many ATP are gained; how many NADH + H+ are formed; where are the NADH + H+ sent to; | 4 ;c02 molecules; 2; 6; the electron transport system |
| aerobic respiration: krebs cycle: summary- why are the 6 NADH + H+ sent to the electron transport system; how many FADH2 is formed; where is FADH2 sent | so they can be utilized for ATP elsewhere; 2; electron transport system as well |
| aerobic respiration: krebs cycle: | |
| coenzyme A is a vit. ___ derivative | vit B |
| aerobic respiration: ETS: aka; how does it get its eletrons from reduced carriers NADH and FADH2; | electron transport system; these reduced carriers are generated by glycolysis and the krebs cycle; |
| aerobic respiration: ETS: how many NADH + H+ molecules were produced from glycolysis; how many NADH + H+ molecules were produced from transition reaction; how many NADH + H+ molecules were produced from krebs cycle; | 2; 2; 6 and 2 FADH2 molecules; |
| aerobic respiration: ETS: location; what are the initial substrates from 1 glucose molecule | cell membrane; 10 NADH + H+ and 2 FADH2 molecules (these are all the ones sent from glycolysis, transition reaction and Kreb's cycle) |
| aerobic respiration: ETS: def of chemiosmosis; hydorgen ions are pumped outside the cytosol between cell ___ and cell ___; what kind of concentration gradient does this create | a process where hydrogen ions are pumped across a cell membrane to form a hydrogen ion gradient; membrane and wall; higher one in extracellular fluid then next to cell membrane and cytosol; |
| aerobic respiration: ETS: what molecules process the electrons from teh hydrogen atoms; where are cytochromes located; what are components of hyodrogen atom; so what portion of hydrogen atom does cytochromes process | the cytochromes; in cell membrane; one proton and one electron; the elctron |
| aerobic respiration: ETS: the cytochromes also play a role in pumping what; | hydrogen ions (protons across the membrane) |
| aerobic respiration: ETS: starting with one NADH molecule- what happens as it approaches the cell membrane; when electrons are cleaved off what is released; where do the protons go when they are released; | an enzymatic reaction occurs were the pair of electrons are cleaved off molecule; ionized NAD; up to cell mebrane waiting to be pumped across; |
| aerobic respiration: ETS: starting with one NADH molecule- once electrons are given up by the NADH molecule what happens to coenzyme; electrons go to 1st what; 1st cytochrome pumps protons across what into what | it is recycled and used again for cellular respiration; cytochrome; cell membrane the extra cellular fluid; |
| protons aka | hydrogen ions |
| aerobic respiration: ETS: starting with one NADH molecule- so as the protons bind to first cytochrome it is __; after it is reduced it is what | reduced; oxidized |
| when anything is reduced (gained electrons) it has to be what; this is aka | oxidized; redux |
| aerobic respiration: ETS: starting with one NADH molecule- after 1st cytochrome what does next one do; how many sets of chromosomes does this process go through; the last cytochrome gives up the pair of electrons to what molecule | repeat process; 5 sets; oxygen |
| aerobic respiration: ETS: starting with one NADH molecule- so cytochrome becomes reduced when it binds to ____; it becomes oxidized when it released what | hydrogen ion; hydrogen ions |
| aerobic respiration: ETS: starting with one NADH molecule- what happens when the pair of electrons bind to 02; is the oxygen molecule neg. or pos. charged; the O2 binds to protons then to form what; | the O2 becomes ionized; neg; H2O |
| aerobic respiration: ETS:starting with one NADH molecule- so hydrogen ions are pumped from __cellular fluid to __cellular fluid; what is the final electron acceptor here; how much ATP is released from 1 NADH;how much from 1 FADH2;so 1 glucose=__ATP in ETS | intracellular to extra cellular fluid; oxygen; 3 ATP; 2 ATP; 34 ATP |
| aerobic respiration: ETS: starting with one NADH molecule- where is there an excess of protons; where do these excess protons go through; protons can move quickly through the pump with the help of what enzyme; this pumps out __ | in the extra cellular fluid; the ATP pump; ATP synthase; ATP; |
| aerobic respiration: ETS: starting with one NADH molecule- why does FADH2 only produce 2 ATP instead of 3 like NADH; | b/c it is unable to bind to the 1st cytochrome |
| aerobic respiration: summary of ATP formation: glycolysis forms how many ATP; how many NADH + H+ are sent to ETs; transition reaction forms how much ATP; how many NADH + H+ are sent to ETS; Kreb's cycle forms how many ATP; | 2 ATP; 2; 0 atp; 2 sent to ETS; 2 ATP |
| aerobic respiration: summary of ATP formation: KRebs cycle sends how many NADH + H+ to ETS; what else does kreb's cycle send to ETS; ETS produces how many atp;one glucose molecules yields a total of __ ATP | 6; 2 FADHs; 34; 38 |
| aerobic respiration: what is the only process that uses the carrier enzyme FADH | the krebs cycle |
| aerobic respiration: ETS: as transport carriers shuttle electrons what happens with the protons; | they are actively moved from the cytoplasm to to the periplasmic space between the membrane and cell wall; |
| other carb energy sources: disaccharides and polysaccharides need to first be hydrolized into what; monosaccarides are chemically _____ before they can enter glycolisis are various starting points; carbs always enter aerobic respiration where | monosaccarides; modified by addition of a phosphate ; in glycolysis |
| proteins as energy source: proteins are long chains of ___; long chains of polypeptides are aka; polypeptides cannot enter___ the way they are; what is 1st step in preparing polypeptides to enter aerobic respiration | polypeptides; amino acids; aerobic respiration processes; |
| proteins as energy source: diagramming generic amino acid- what is carbon in center called;proteins as energy source: what is region to bottom of central carbon called; what is NH2 called; | central carbon; what is COOH on right side called; carboxyl group; variable region; amino group; |
| proteins as energy source: what is first step in getting protein ready for aerobic respiration; first the ___ group is removed from the amino acid; by what reaction is the amino group removed; where does the amino group go; what happens w/ rest of AA; | deamination; amino group; and enzymatic reaction; off to synthesize other amino acids; this deaminated portion enters the carbohydrate pathway; |
| proteins as energy source: so the deaminated portion enters what part of the carbohydrate chain; | this depends on the carbon backbone of the molecule (2 or 3) |
| energy from fats: a fat molecule is aka; what first takes place to break down larger molecule; hydrolysis breaks down larger molecule to what; | triglyceride; hydrolysis; smaller molecules; |
| energy from fat: so when a triglyceride is hydrolysized it breaks into what molecules; what is the glycerol made of; how many carbons does glycerol have; glycerol can enter carb pathway where | glycerol and 3 fatty acids; carbon hydrogen and oxygen; 3 carbons; as a 3C molecule in glycolysis |
| energy from fats: the 3 fatty acids are made of long ___ chains; the fatty have to be further processed by what reaction; def of beta oxidation reaction; once broken down into 2 carbon fragments where does this enter into carb pathway | hydrocarbon chains; beta oxidation; breaking down fatty acids into 2 carbon fragments; acetyl |
| energy from fats: fatty acids can produce more ATP than carbs is this true | yes |
| anaerobic respiration: what is the difference in the final electron acceptor; do these bacteria use glycolysis, krebs cycle, ets, transition reaction?; | in that it utilizes oxygen containing ions rather than free oxygen as the final electron acceptor; yes |
| anaerobic respiration: give example of electron acceptor; give example of bacteria that is a nitrite producer; sulfite ions produce what; | nitrate ion plus the electron acceptor equal nitrite or sulfite ions; E. coli; hydrogen sulfide -rotten egg smell |
| fermentation: fermentation produces ATP in the absence of what; what carbohydrate process does fermentation always follow after; def of fermentation; do fermentative reactions produce ATP; | cellular respiration; glycolysis; the incomplete oxidation of glucose or other carbs in the absence of oxygen; no; |
| fermentation: fermentation takes the 2 NADH molecules produced in glycolysis and does what with them; do transition reaction, krebs cycle, ets occur in a cell using fermentation?; | consumes them and releases ionized NAD; no; |
| fermentation: purpose- regeneration ionized __; allows glycolysis to continue by doing what | NAD; consuming end products; |
| fermentation: using streptococcus lactis- this bacteria uses fermentation and glycolysis to produce what; the 2 pyruvic acid molecules from glycolysis are used as __ acceptor; what is end product here | ATP; electron; 2 lactic acid molecules (pyruvic reduced state) |
| glycolysis, transition reaction, krebs cycle and ets is called akak | the carbohydrate pathway |
| fermentation: the only way a cell using fermentation can survive and produce ATP is by what; | glycolysis; |
| fermentation: ex: yeast cells- first what occurs; they fermentation reaction here goes through how many steps; what is end product; what is substrate after pyruvic acids; 2 acetaldehyde molecules are reduced and form what ; what is final electron acceptor | glycolysis; 2; alcohol; 2 acetaldehyde; ethanol; ethanol |
| cellular respiration in eukaryotic cells- protozoa, algae and fungi-where is glycolysis located; where is fermentation reactions; where do transition reactions or krebs cycle located; where is ETS located; | in cytosol; in cytosol; in matrix of mictochondrion; in cristae of mitochondrion; |
| def spontanious mutation | |
| def induced mutation | |
| def mutagen | |
| def carcinogen | |
| def ames test | |
| def conjugated | |
| def transformation | |
| def transduction | |
| def sex pilus (conjugation pilus) | |
| Genoeme: def; most of the genome exists in what form; genomes of cells are composed of what; each person has a unique __ | this is the sum total of genetic material of a cell; chromosomes; DNA (in viruses it is RNA; genome |
| chromosome: def; what is eukaryote chromosome like; what is prokaryote chromosome like; | a discrete cellular structure composed of a neatly packaged DNA molecule; a DNA molecule tightly wound around histome proteins; it is condensed into a packet like histone proteins |
| chromosomes: eukaryote oens found where;how many strands of chromosome do bacteria have | in nucleus; single double stranded |
| chromosomes: they contain baisc information packets called ___; | genes; |
| genes: def; where is info for cell function found; what does it have to make protein or RNA; | the fundamental unit of heredity responsible for a given trait in an organism; in the gene; a code; |
| genes: what are the 3 categories; structural genes code for what; regulatory genes control what; the sum of all these types of genes is the genetic ___; | strutural genes; regulatory genes, genes that code for RNA; proteins; gene expression; makeup |
| genes: the genetic makeup is aka; the phenotype can change depending on what; | phenotype; which henes are turned on or expressed |
| where is dna found in prokaryote; where is dna found in the eukaryote; where is dna found in a virus | chromosome in nucleus, mitocondria, chloroplast, plasmids ;chromosome and plasmids; core of and capsid |
| bacteria chromosomes: most bacteria have how many single circular double stranded chromosomes; the chromosome of bacterial cell takes up how much space of cell; | 2; 1/3rd |
| DNA code: who discovered DNA and when; what type of acid is DNA; DNA consists of 2 strands combined to form what; | james watson and francis crick 1953; nucleic acid; a double helix; |
| DNA structure: how many strands does it have; the strands are antiparralel what does that mean; what is the basic unit of DNA; | 2 (double); one side of the helix runs opposite direction of the other strand; the nucleotide; |
| DNA- nucleotide: what is it made up of; how many types of DNA nucleotides are there; what is the backbone of DNA; what attaches to the deoxyribose; how many nitrogenous bases are there; name the nitrogenous bases | phosphate,deoxyribose sugar and nitrogen base; 4 types; the phosphate group and deoxyribose groups; nitrogenous bases; 4; guanine, cytosine, adenine, thymine |
| dna nucleotide: each deoxyribose bonds covalently with how many phosphates; so the bonds of deoxyribose are either to the what 2 carbons; how to the nitrogen bases pair up; A and T make __ hydrogen bonds; G& C make __ hydrogen bonds; | 2; 3 prime or five prime; AT and GC; double; triple; |
| DNA- nucleotide- so the bases are joined by what; what base pairs are most stable, why; | the hydrogen bond; CG b/c they have a triple hydrogen bond |
| DNA structure: so one strand runs from a 5 prime to __ prime orientation and the other one runs from a 3 prime to a __ prime | 3 and 5; |
| nitrogenous bases: so if there are a large number of AT bases why does this present a problem; | this is an area that is weaker making it easier to break apart; |
| DNA structure: the arrangment of nitrogenous bases are important for what 2 reasons; how does maintain the code; how does it provide variety | maintainance of codings for replication and providing vareity; consistant base pairs guarentees that code will be retained during cell growth; this has info the produce RNA and thus phenotype of the cell; |
| DNA replication- how nucleotides are added: replication requires how many diff. enzymes | 30; |
| DNa replication: def | this is the process of codes being duplicated and passed to offspring |
| DNa replication- enzymes: what does helicase do; what does primase do; what does DNA polymerase III do; what does DNA polymerase I do; what does ligase do; what doe gyrase do | unzips DNA helix; synthesizes an RNA primer; adding bases to the new DNA chain nad proof reads chain for mistakes; removes primer, closes gaps, repaires mitchmatching; final binding of errors; supercoils it |
| DNA replication: what is 1st step; when the hydrogen bonds are unzipped between base pairs what happens; how are two new strands synthesized | to uncoil the parent DNA molecule; the strands are separated and the nucleotides are exposed; by attaching the correct complementary nucleotides to each single stranded template |
| DNA replication- each daughter molecule will be identical to what; what is the main enzyme in replication; | the parent in composition; DNA polymerase III |
| replication- DNA polymerase II- can it begin a synthesizing a chain of nucleotides; it can only continue to add nucleotides how; | no; to an already existing chain and in only one direction; |
| DNA- replication: daughter molecule has one ore two completely new strands; def of origin of repliation; why is it called semiconservative replication | one; site that serves as the place where replication will be initiated; because only one strand is completely new the other is the parent strand; |
| DNA- replication: replication begins at what base pair rich section; helicase untwists what; helicase breaks what; the untwisting and break of hydrogen bonds creats what | AT; the helix; hydrogen bonds; 2 replication forks |
| DNA- replication: since the area of replication is AT rich it requires less or more energy to separate strands the GT bond; | less energy; |
| DNA- replication: primase- what is formed at teh origin of replication; what recognizes the RNA primers; | an RNA primer; DNA polymerase III; |
| DNA- replication: DNA polymerase III- this adds what to parent strand of DNA; what is a leading strand; def lagging strand; lagging strand AKA; | DNA nucleotidesthis is formed as a continuous complete strand moving toward the replication fork; not sunthesized continuously and moves away from the replication form; okazaki fragments; |
| DNA- replication: when is the lagging strand completed; what 2 enzymes can make repairs; | when the enzyme fills spaces between the okazaki fragments with correct nucleotides; DNA polymerase I and III |
| DNA- replication: replication fork is located where; lagging stran goes to or away from replication fork; leading strand goes to or away from replication fork; | in the middle in between the DNA polymerase III;towards; away |
| DNA replication: why does it occur before binary fission; also in cells able to produce endo spores. | so daughter cell would have replicated chromosome; |
| central dogma: what is it; what is new in recent years in regards to RNA; | that genetic info typically flows from DNA to RNA to protein;some RNAs are now used to regulate gene function also many of genetic malfunctions that cause human disease are found in these regulatory RNA segments |
| DNA is used to synthesis what; what is it called when DNA 1st synthesizes RNA; information contained in RNA is used to produce what; RNA producing protein is called what; | RNA; transcription; protein; translation; |
| messenger RNA: def; its synthesis is similar to what other synthesis; the message of transcribed strand is later read in a seriers of ___; the triplets are aka; this is a complementary strand to what; each codon codes for what | this is a readable copy of DNA, a transcript of a structural gene or genes in the DNA; the synthesis of the leading strand during DNA replication; triplets; codons; dna; amino acids |
| transfer RNA: this is a copy of what; | a specific region of DNA; |
| when a triplet code is transcribed and translated it dictates the type and order of what | amino acids in a polypeptide chain (protein chain) |
| a proteins primary structure is determined by what | the order and type of amino acids in the chain |
| the DNA molecule is a continuous chain of base pairs, but must be interpreted how; each triplet is copied to what; the mRNA codons translate into what; what is the ration of base pairs to amino acids | in groups of three base pairs; an mRNA codon; one amino acid; 3:1 |
| RNA: what is the full name of it; what base does it not contain; what is the base that it does contain; uracil pairs with what; what is the sugar in RNA; what is the sugar in DNA | ribonucleic acid; thymine; uracil; adenine; ribose; deoxyribose |
| what is the key to translation | transfer RNA |
| transfer RNA: this contains sequences of bases that form ___ bonds with what; since it forms hydrogen bonds with same section of tRNA strand what happens | hydrogen bonds with complementary sections of the same tRNA strand; the molecule bends back on itself into hairpin loops (looks like a key) |
| tRNA: what is the final structure called after the bending hairpin loops; this transpates the RNA language into what language; what is the bottom loop of the cloverleaf exposing the triplet called; | cloverleaf; the protein language; the anticodon |
| tRNA: what id the anticodon; what is the binding site on teh opposite end of the molecule for; | thisdesignates the specificity of the tRNA and complements mRNAs condons; the amino acid that is specific for that anticodon |
| tRNA: for each of the 20 amino acids there is at least how mant specialized type of tRNA to carry it ; where does the tranfer of genitic information form mRNA to tRNA take place | one; at the ribosome |
| the ribosome: the is a moblie molecular factory for what; what is it composed of; what type of molecule is it | translation; tightly packed rRNA and protein; a long polynucteotide molecule |
| ribosome: the interaction of proteins and rRNA creates what; prokaryotic ribosomes are considered __ s | the 2 subunits of teh ribosome that engages in final translation of teh genetic code; 70s |
| stages of transcription: what are the 3 stages; the tranfer of genitic info into and RNA molecule is initiated by what; what does RNA polymerase do; | initiation,elongation, termination; RNA polymerase; binds to DNA, unwinds it and synthesizes RNA |
| transcription: initiation- initiation requires RNA polymerase to recognize what on a gene; the promotor region has how many sets of DNA sequences; what is primary function of promotor region; | region called the promotor region; 2; to provide a position for initial binding of RNA polymerase |
| transcription: initiation- RNA polymerase first begins to do what to DNA; what strand of DNA is transcribed; def of trempate strand; def of nontemplate strand; is the promotor sequence transcribes as part of the final mRNA molecule; | unwind the DNA strand; the template strand; the strand the carries a message that can be translated in to a protein; serves a genetic function but not as a message for protein structure; no |
| transcription: what is usually the first DNA triplet; so since RNA will have uracil not thymine what is the first codon on the mRNA; def of elongation; RNA polymerase adds complementary ___ the form the single stranded mRNA | TAC; AUG; the RNA polymerase moves the transcription bubble forward exposing subsequent sections of DNA; nucleotides |
| transcription: termination- the RNA polymerase continues transcribing until it reaches what; what is at the termination site; what is released at the termination site; the completed mRNA goes immediately to what; what happens to the DNA after this | a termination site; the stop codon; the mRNA transcript; translation; it is rewound into its original configuration |
| what is first stage of gene expression; what is second stage of gene expression | transcription; translation |
| tranlation: all of the elements needed to synthesize a protein are brought together where; what are the 5 stages of translation | on the ribosomes; initiation, elongation, termination, protein folding and protein processing |
| translation: where is the site of this process; | prokaryotic ribosome |
| ribosome: how many subunits does it have; what is the small subunit for; the large subunit has how many sites; what are the names for the 3 sites in the large subunit; | 2; binding site for mRNA; 3; E,P,A |
| ribosome: what does site E do; what does site P do; what does site A do | exit site for tRNA molecule; peptidyl site for where amino acid is transferred from tRNA to growing polypeptide chain; acceptor site for tRNA molecule to bind to its anticodon to the codon on the mRNA strand |
| translation: when the mRNA molecule leaves the DNA transcription site where is it transported; the small subunit of the ribosome what; the ribome scans the mRNA by moving how; when does translation begin | to the ribosome; the 5 prime end of the mRNA; in a 5 prime 3 prime direction; when the ribosome encounters a start codon |
| translation: what is usually the start codon; when mRNA is in place of the ribosome what enters with their amino acids; what meets with the mRNA codon site; what happens when the tRNA binds with the mRNA; | AUG; tRNA in teh acceptor site; tRNA anticodon; amino acid is released from tRNA molecule |
| translation: when is the tRNA molecule released from the ribosome; what guides the tRNA to meet with the mRNA; | when it enters the exit site; the P and A site of the ribosome; |
| translation: what are the nonsense, stop or termination codons; once teh triplet code on mRNA is known what all can be known; | uga, UAA, UAG; the original DNA sequance, the complementary tRNA code and the types of amino acids in protein are known |
| why did stop codons get naem of the nonsense codons; | because no tRNA can bind to them |
| translation: what happens when the stop codon is reached; what breaks the bond between the tRNA and polypeptide chain; what does polypeptide chain get reconfigured into once out in cytosol | messenger RNa is released from the ribosome; a special enzyme breaks the bond between the final tRNA and the finished polypeptide chain; a protein |
| codons code for what; | amino acids |
| genetic regulation of protein synthesis and metabolism: why are enzymes regulated; enzymes are produced when; why are enzymes produced only as needed; what is a major form of gene regulation in prokaryotes | to ensure that genes are active only when their products are required; as they are needed; to prevent the waste of energy and materials; opserons |
| operons: def; what are the categories of operons; the category of and aperon is determined by what; | a specific set of genes whose function is coordiated as a single unit; induced or repressible; by how it is affected by the environment within the cell; |
| operon: what does induced mena; what does repressed operon mena; | the operon it turned on by the substrate of the enzyme for which the structural genes code; they contain genes coding for anabolic enzymes and several genes in a series or thurned off by the product synthesized by the enzyme |
| the lastose operon: regulates metabolism for what; what are the 3 important features in this; what is the regulator; what are the 2 components of the control locus; | the E. coli; the regulator,control locus and structural locus; a gene that codes for a protein capable of repressing the operon; promotor and operator |
| lactose operon: control locus- what does promotor do; what happens it the repressor protein is inhibited; | binds RNA polymerase (beginning component of operon); a sequence that acts as an on/off switch for transcription; the operator is on; |
| lactose operon: what is the structural locus | made up of 3 gens each coding for a different enzyme needed to catabolize lactose |
| lactose operon: operon off- in the adsence of lactose a repressor protein attaches to what; when the repressor protein attaches to the operator what happens; suppression of a transcription prevents what | the operator of the operon; this locks the operator; unnecessary synthesis of enzymes for processing lactose |
| lactose operon: operon on- how does lactose become a genetic inducer; the RNA polymerase can now do what; the enzymes produced from translation do what to lactose; what are the 3 enzymes produced; | by attaching to the repressor which loses its grip and falls away; bind to the promotor and initiate transcription; reactions; permease, beta-galactosidose; transacetylase |
| lactose operon: if lactose is added to cells environment it triggers what | the opeeron to turn on |
| lactose operon: it only operates in the absense of what | glucose; |
| mutation means the __ sequence is altered; most times this is what; what fixes the mutations | nucleotide; repaired; enzymes |
| def spontaneous mutation | random changed in the DNA arising from errors in replication |
| def induced mutation | results from eposure to known mutation |
| repairing mutation: dna that has been damaged by UV radiation- how is it repaired; what light sensitive enzyme does the repair | by photoactivation or light repair; DNA photlyase |
| repairs of mutation: excision repair- def; | mutations can be excised by a series of enzymes that remove the incorrect bases and add the correct ones |
| mutations- the ames test- def ; any chemical that is capable of mutating bacterial DNA can mutate what | a rapids screening test that detects chemicals with carcinogenic potential; mammalian DNA |
| AMES test: procudure- what culture is inoculated on 2 agar plates; what are the agar plates; what happens with control plate; what happens with test plate | salmonella bacteria that is histine -; histine free medium; it is incubated and contains no test chemical just the organism; contains organism and chemical and then is incubated |
| Ames test: test plate after incubation will have colonies after incubation will have ben mutated and now will form what; what will control plate look like after incubation | histidine; there will not be colonies (maybe a few from spontanious mutations) |
| ames test: what is end purpose | the chemical will determined to be a mutigen capable of mutating human DNA |
| def of carcinogens | chemicals the produce an increased incidence of back mutation |
| DNA recombination: def; the recipient organism now has how many types of DNA; what is the end result; what is new strain called | when one bacterium donates DNA to another bacterium; 2; new strain differernt from donar and recipient; recombinant organsim |
| transmission of genetic material in bacteria: this usually involves what type of DNA; plasmids can replicate independently of what; what are the 3 types of genetic recombination; | the plasmids or chromosomal fragments; the bacterial chromosome; conjugation, transformation, transduction |
| DNA recombination: conjugation- def; can gran + or gram - conjugate; is thsi exchange direct of indirect | a mode of genetic exchange in which a plasmid or other genetic material is transferred by a donor to a recipient via a direct connection; both; direct |
| DNA recombination: conjugation involving F factor transfer- the pilus of the donar cell attaches to what; what is donor called; what does F stand for; what is recipient called; | the receptor on the recipient cell and draws the 2 cells together; f+ cell- it has F factor; fertility factor the plasmid in F+; F- because it lacks that F factor |
| DNA recombination: conjugation involving F factor transfer- what produces the pilus the F+ or F-; the cells have to be very similar why; why does the F+ shorten the pilus between the 2 cells; | F+; in order for them to attach to eachother; so the connection can be stablelized |
| DNA recombination: conjugation involving F factor transfer- why does a pore form between the F+ amd F- cell; what happens with the F+ factor; | so the cytosol is continuous between the 2 cells; one strand unwinds and crosses through the pilus and enters the F- cell; |
| DNA recombination: conjugation involving F factor transfer- what happens when F factor enters F- cell; what happens to the strand left over in the F+ cell; | it is replicated; that is also replicated; |
| DNA recombination: conjugation involving F factor transfer- at the end both cells are F+ orF-; the F factor (plasmid) is not essential for ife of cell but it can do what | F+ - capable of conjegating with similar cells; account for pathogenic charecteristics |
| DNA recombination: conjugation involving Hfr transfer- what does Hfr stand for; what is an Hfr cell; is this common or rare; | high frequancy transfer rate; one that had an F factor in its cytosol but F factor was combined into the cells chromosome; rare |
| DNA recombination: conjugation involving Hfr transfer- first the Hfr cell develops a what; the pilus connects to what type of cell; the Hfr cell shortens pilus just like F factor transfer but then enzymes do what | pilus; and F - cell; effect area on chromosome; |
| DNA recombination: conjugation involving Hfr transfer- why do the enzymes have to work on the chromosome; do you get partial or full copy of the chromosome occur | so transmission of part of the chromosome (just a section) can occur; just part |
| DNA recombination: conjugation involving Hfr transfer- now the F- minus cell gained genetic material it is called what; why is it still considered an F - cell | a recombinent F - cell; b/c it did not gain all of the genetic material |
| DNA recombination: biomedical importance of conjugation: F factors can bear genes that are resistant to what; so one bacteria can have multiple what; what is the name for plasmids that are resistant; | antibiotics; resistance to antibiotics; R plasmids; |
| Griffiths expirement in transformation: what was it; when did it occcur; one strain produced a what; the capsulated strain caused what; would the uncapsulated strain produce pna; | it was the first to show transformation occurring between 2 diffent strains of Strep. pneumoniae; 1928; capsule; pneumonia in animals; no; |
| Griffiths expirement in transformation: process- the smooth strain was given to what; what happened to mice with smooth (capsulated strain) strain; what was done with rough (uncapsulated strain); next the scientist killed what strain before giving to mice | mice; they died; the mice lived; the smooth strain |
| Griffiths expirement in transformation: process- did the mice live with killed smooth strain; then the rough strain was combined with heat killed smooth strain and gave it to mice- did the mice die or live; what did this prove | yes; they died; bacterial DNA is released in fragments from dead bacterial cells and the other cells (rough strain) incorportated fragments into their cells and created capsules themselfs |
| Griffiths expirement in transformation: this proved what; def of compenent cells ; | that DNA released from a killed cell can be acquired by a live cell; ce;;s capable of accepting genetic material; |
| DNA recombination: generalized transduction: what is a bacterialphage; the phage does what; in replication on the virus accidently does what; cell A lyses and releases what | a virus that serves as a carrier of bacterial DNA from one bacterial cell to another of the same species; it injects the viral DNA to cell A and the virus is reproduced; incorperates a segment of bacterial DNA by mistake into virus particles;alteredphages |
| DNA recombination: generalized transduction: the mature altered phages penetrates other host cells and injects DNA from what; what does cell B do with this DNA; what happens with defective virus | cell A rather than the viral nucleic acid; it recombines with its own DNA; it is unable to cmplete lytic cycle |
| basic elements and applications in genetic engineering: what are they | tools and technics, recombinant DNA technology, biochemical products of recombinant DNA technology, genetically modified organisms, genetic treatments, genome analysis |
| recombinant DNA technology: def; what is the cloning vector; the cloning vector inserts what into cloning host cell; why is this important; | removes genetic material from one organism and combines it with that of a different organism; the plasmid or virus; the DNA; human insulin is produced by E. Coli |
| protein products from recombinant DNA tech: purpsoe of interferons; interleukins; human growth hormone; hep B vaccine; | used to treat cancerm MS, viral infections like hepatitis; regulates immune function of WBC and cancer tx; dwarfism; used for Type B meningitis |
| dna replication:okazaki fragments are formed in the lagging strand yes or no; do these fragments run in a 3' to 5' orientation or a 5' to 3 orientation | yes; 3- to 5' orientation |
| high frequency recobination cells (HFR cells) arine from the f- or f+ cell when the R plasmid is incorporated into the bacterial chromosome | the F- |
| the leading strand during DNA replication orients to the 5' to 3' direction or to the 3' to 5' direction | the 5' to 3' direction |
| which group of viruses; ones with double stranded DNA as their genetic information or ones with single stranded RNA as genetic material; is more likely to repair its genetical material in a eukaryotic host cell | double stranded DNA virus |
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