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| 4703526937 | What are the two amino acid functional groups? | amino group (NH2) carboxyl group (COOH) | 0 | |
| 4703533528 | chiral centers | have four different groups attached to it, are optically active All a.a.'s are chiral except one | 1 | |
| 4703534357 | what is unique about glycine? | a achiral molecule, has an hydrogen molecule as the R-group and is the only amino acid that isn't chiral, doesnt have an (S) or (R) configuration |  | 2 |
| 4703539758 | D-amino acids | enantiomers of the amino acid that has amino group on the right | 3 | |
| 4703554413 | What is unique about Cysteine? | only amino acid that doesn't have (S) configuration (like all other a.a.) b/c it has an R-group that has higher priority than carboxyl group it has a (R) configuration instead | 4 | |
| 4703539757 | L-amino acids | enantiomers of the amino acid that has amino group on the left only L-a.a. are used by cells | 5 | |
| 4703556203 | Nonpolar, nonaromatic side chains amino acids (7) Hydrohphobic | Glycine, Gly, G Alanine, Ala, A Valine, Val, V Leucine, Leu, L Isoleucine, Ile, I Methionine, Met, M Proline, Pro, P | 6 | |
| 4703556623 | nonpolar, aromatic side chains amino acids (3) Hydrohphobic | tryptophan, Trp, W phenylalanine, Phe, F tyrosine, Tyr, Y | 7 | |
| 4703557040 | polar side chains amino acids (5) Hydrohphilic | serine, Ser, S threonine, Thr, T asparagine, Asn, N glutamine, Gln, Q cysteine, Cys, C | 8 | |
| 4703585559 | Negatively charged acidic side chains (2) Hydrohphilic | aspartate, Asp, D glutamate, Glu, E | 9 | |
| 4703586232 | Positively charged basic side chains (3) Hydrohphilic | lysine, lys, L arginine, Arg, R histidine, His, H | 10 | |
| 4705665918 | Absolute configuration | 3D model of the arrangement of atoms | 11 | |
| 4705673978 | amphoteric species | Amino acids are this because they can either accept or donate a proton. it helps form micelles and phospholipid bilayers b/c it has hydrophilic and hydrophobic regions | 12 | |
| 4705675336 | The behavior of amino acids is based on | pH at low pH (acidic), ionizable groups tend to be protonated ; at high pH (basic), ionizable groups tend to be deprotonated if the pH is less than the pKa, it will be protonated if the pH is higher than the pKa, it will be depronated | 13 | |
| 4707248684 | Bronstead lowry base | proton acceptor | 14 | |
| 4707248685 | Bronstead lowry acid | proton donor | 15 | |
| 4707254624 | lewis acid | electron pair acceptor | 16 | |
| 4707254698 | lewis base | electron pair donor | 17 | |
| 4707289363 | Lewis bases and Bronstead Lowry bases are the same in a reaction because | a proton acceptor is the same as an electron pair acceptor | 18 | |
| 4707291569 | Is the Lewis Base an electrophile or nucleophile | Nucleophile | 19 | |
| 4707420731 | pKa equation henderson equation | pKa = -logKa pH = pka + log [A] base/[HA] acid | 20 | |
| 4707421848 | A strong acid has a ____ Ka value, a ___ pka value equilibrium lies to the ____ | high, low, right | 21 | |
| 4707443477 | Nucleophiles are negative or positive? | negative | 22 | |
| 5772267782 | Alkaline pH value | Basic pH | 23 | |
| 5772267783 | Isoelectric point (pI) | pH where the molecule is electrically neutral pI = (pka1 + pka2) / 2 | 24 | |
| 5772267784 | Peptide bond formation | Condensation/dehydration reaction The carboxyl 'OH' and amino 'H' form water | 25 | |
| 5772267785 | Peptide bond breakage | Hydrolysis reaction Add an 'H' to amide Nitrogen and an 'OH' to the carbonyl carbon | 26 | |
| 5832913182 | Hydrolysis | adds water to break C-N bond Carbonyl side gets -OH, forming a carb acid Nitrogen picks up an -H, forming an amine | 27 | |
| 5772267786 | Globular | Spherical (globe) shaped proteins Ex: myoglobin Caused by tertiary and quaternary structures folding | 28 | |
| 5772267787 | Fibrous | Long strand (sheet-like) proteins Ex: collagen | 29 | |
| 5783494099 | When an hydrophobic a.a. dissolves it can't form ___, entropy ____ and is unfavorable delta G is ____ | h-bonds, decreases, is greater than zero | 30 | |
| 5772267788 | Liproproteins | Proteins with lipids | 31 | |
| 5772267789 | Glycoproteins | Proteins with carbohydrate | 32 | |
| 5772267790 | Nucleoproteins | Proteins with nucleic acids | 33 | |
| 5772267791 | Prosthetic group on hemeglobins | Heme | 34 | |
| 5772267792 | Prosthetic groups are | Coenzymes and cofactors | 35 | |
| 5772267793 | Cofactors | Metal ions, inorganic molecules, minerals | 36 | |
| 5772267794 | Coenzymes | Vitamins (FAD, NAD+, CoA) and organic molecules | 37 | |
| 5772267795 | The graph of a molecule that follows Michealis menten is | Hyperbolic | 38 | |
| 5772267796 | Oxidoreductases | Enzyme that catalyze redox | 39 | |
| 5772267797 | Transferase | Enzyme that catalyze movement of functional group | 40 | |
| 5772267798 | Hydrolase | Enzyme that catalyze breakdown of molecules using water | 41 | |
| 5772267799 | Lyases | Enzyme that catalyze cleavage of molecules without water | 42 | |
| 5772267800 | Isomerase | Enzyme that catalyze rearrangement of bonds in a molecule | 43 | |
| 5772267801 | Ligases | Enzyme that catalyze addition b/w large and similar molecules | 44 | |
| 5772267802 | Haloenzymes | Enzymes that are bounded to cofactor | 45 | |
| 5772267803 | Apoenzymes | Enzymes that are not bounded to cofactors | 46 | |
| 5772267804 | Zymogens | Control enzymes by being the in the inactive form of enzymes | 47 | |
| 5783495137 | What do enzymes do | help reach the transition state easier by lowering the activation energy | 48 | |
| 5783495651 | induced fit | the enzyme's shape is changeable and changes in order to fit the substrates unique shape | 49 | |
| 5783498263 | Vmax | it is the max velocity of a reaction; the saturation point of enzymes | 50 | |
| 5783498756 | When does Km = [S] | when the reaction is at half the Vmax | 51 | |
| 5783499302 | The substrate and enzyme have high affinity for each other when the Km is ___ | low | 52 | |
| 5783500378 | optimal pH of gastric enzymes is ___, pancreatic enzymes ___. | 2, 8.5, | 53 | |
| 5783501464 | optimal of enzymes is ___ degrees C, ____ degrees F, and ____Kelvin | 37, 98.6, 310 | 54 | |
| 5783501648 | Celsius to F formula | Temp (F) = Temp (C) * 9/5 + 32 | 55 | |
| 5783503296 | Celsius to Kelvin formula | C = 273 + K | 56 | |
| 5783499706 | The Km can be altered by doing what to [E] and [S] | nothing, the Km can't be altered this way | 57 | |
| 5783508522 | Competitive inhibition | Adds more substrate to compete to bind to the active site. This increases the Km because the substrate increases | 58 | |
| 5783508942 | noncompetitive inhibition | Binds equally (same affinity) to the allosteric sites of the enzyme and enzyme substrate complex When it binds, it changes the enzyme confiormation so that the substrate can't bind to enzyme. This decreases Vmax b/c there are less substrates and enzymes able to react, thus less reactions It does NOT effect any ES complex - thus Km is unchanged | 59 | |
| 5783510984 | mixed inhibition | Binds unequally (different affinity) to the allosteric sites of the enzyme and enzyme substrate complex if it has higher affinity binding to the enzyme over the ES complex then the Km increases (which means overall, it has a lower affinity bc high Km = low affinity) It has a lower Km vise versa which means high affinity in the reaction | 60 | |
| 5783574927 | uncompetitive inhibition | Inhibitor only binds to the ES complex and prevents the release of enzyme thus making less products when bound and decreasing Vmax Reduces the amount of ES complexes thus reduces [S] and thus lowers Km reduced the amount of available ES we have Vmax also lowering | 61 | |
| 5783578205 | Factors affecting Vmax | Amount of free E or ES available to complete the reaction at high [S] | 62 | |
| 5783578934 | Characteristics affecting Km | When there's lower ES complex available -its about the affinity b/w substrate and enzyme | 63 | |
| 5783594440 | Reactions with enzymes have ___ temperature | lower | 64 | |
| 5783596762 | Structural Proteins | proteins that contain motif structures | 65 | |
| 5772267805 | Motif | A repetitive structure of structural proteins that involve secondary elements | 66 | |
| 5772267806 | Collagen | Makes up connective extracellular tissue Contains Gly residues Provides strength and flexibility Forms a Rt handed helix | 67 | |
| 5772267807 | Elastin | Makes up connective extracellular tissue Stretches and recoiles | 68 | |
| 5772267808 | Keratin | Found in epithelial cells Make up hair and nails | 69 | |
| 5772267809 | Actin | Helps provide a pathway for the flow of motor proteins down the actin filament Makes up microfilaments | 70 | |
| 5772267810 | Tubulin | Makes up microtubules Intracellular transport via kinesin and dynein Involved in mitosis and meiosis | 71 | |
| 5783595831 | Motor proteins | interact with actin or tubulin muscle contraction and cellular movement | 72 | |
| 5772267811 | Myosin | The prime motor protein that interacts with actin Cellular transport | 73 | |
| 5772267812 | Dynein/kinesin | Interact with tubulin Vesicles transport | 74 | |
| 5783598879 | Hemoglobin | is a binding protein | 75 | |
| 5783599302 | cell adhesion molecule | on the cell surface that help bind to other cells or to extracellular matrix are integral membrane proteins | 76 | |
| 5772267813 | Cadherins | is a cell adhesion molecule they hold similar cell types together mediate calcium dependent cell adhesion ex: epithial cells | 77 | |
| 5783604703 | integrins | is a cell adhesion molecule communicate with extracellular matrix and is involved in cellular signaling and function (cell division, apoptosis, WBC migration) | 78 | |
| 5783604704 | Selectins | is a cell adhesion molecule found on WBC and endothial cells that line blood vessels, play a role in defense against microorganisms, WBC migration and inflammation | 79 | |
| 5783606709 | Immuniglobulins | any of a class of proteins present in the serum and cells of the immune system, that function as antibodies. | 80 | |
| 5783606866 | Antiboides (immunoglobulins) | the most abundant protein in the immune system They neutralize bacteria and recruit other cells to eliminate the, such as macrophages held together by disulfide bonds and N.C. bonds Bind to only to SPECIFIC antigens | 81 | |
| 5804451777 | column chromatography | alumina beads are used to separate proteins based on their size and polarity the less polar proteins elude first down the column (the beads can be changed so it can separate based on polarity, pH, salinity) | 82 | |
| 5804465797 | anion exchange chromatograhy | the beads are POSITIVELY charged so that they attract the opposite charged compounds, an ion exchange chromatography example | 83 | |
| 5804471884 | cation exchange chromatograhy | the beads are NEGATIVE | 84 | |
| 5804473426 | size exclusion chromatograhy | large proteins elude down the column faster because they can't fit into the tiny pores but the smaller ones do | 85 | |
| 5804480520 | affinity chromatography | the beads are coated with a receptor that binds to a specific protein ex: Nickel - His tage Antibodies - Antigens Enzyme - substrate | 86 | |
| 5783607011 | opsonization | when antobodies bind to antigens and marks pathogen for destruction | 87 | |
| 5784552771 | microphages | digest clumps of antigens and antibodies binded together | 88 | |
| 5784557696 | enzyme linked receptors | membrane receptors function as enzymes when a ligand binds | 89 | |
| 5784558059 | G protein Gq | stimulates phospholipase C which cleaves phosholipid to form PIP2 which is cleaves into DAG and IP3 (opens Ca2+ channels) | 90 | |
| 5784559557 | Concentration determination Assay | uses UV spectrum to determine the amount of protein in a sample by colorimetric change. Proteins with aromatic rings (polyenes) are useful here | 91 | |
| 5784560532 | Bradford protein Assay | Determines protein concentration through the mixture of the protein and coomassive Brilliant Blue dye. When the dye is deprotonated (makes contact with protein) the color changes from brown/green to blue | 92 | |
| 5784562417 | X ray chrystallography | determines the protein structure by turning the protein into a crystal, x ray source measures the diffraction patttern, solve the phase problem and the pattern can be mapped out into a electron density map. Then this shoes the exact arrangement of the atoms in the crystal. | 93 | |
| 5784566091 | NMR | The process uses that principle that nuclei have spin states and if a magnetic field is applied, an energy transfer is possible between the base energy to a higher energy level The energy transfer takes place at a wavelength that corresponds to radio frequencies and when the spin returns to its base level, energy is emitted at the same frequency. The signal that matches this transfer is measured in many ways and processed in order to yield an spectrum for the nucleus concerned. | 94 | |
| 5804499108 | edman degradation | a technique that determines the primary structure of amino acids. Cleaves N-term and then analyzes through mass spectroscopy | 95 | |
| 5773491107 | D-fructose | is an ketohexose sugar CH2OH =O H OH OH CH2OH | 96 | |
| 5773491108 | D-glucose | aldohexose sugar CHO OH H OH OH CH2OH | 97 | |
| 5773493777 | D-galactose | aldohexose sugar CHO OH H H OH CH2OH | 98 | |
| 5773493818 | D-mannose | aldohexose sugar CHO H H OH OH CH2OH | 99 | |
| 5784793299 | how to determine the number of stereoisomers | 2^n, n = # of chiral carbons | 100 | |
| 5784793865 | Reducing sugars | have reducing potential because they can be oxidized, any aldose molecule is an example (glucose) | 101 | |
| 5784794093 | Tollens reagent | reduces Ag+ to metallic silver | 102 | |
| 5784794155 | Benedicts reagent | deteccts presence of reducing sugars by turning into red precipitate | 103 | |
| 5784794295 | glucose oxidase | tests for glucose presence | 104 | |
| 5804547166 | nitric acid | a powerful oxidizing agent (oxidizes) | 105 | |
| 5784799321 | Reduction | gains electrons, become more negative and the charge is reduced | 106 | |
| 5784799382 | Oxidation | lose electrons, become more positive and the charge is oxidized | 107 | |
| 5784800714 | Which of these creates a carb. acid under oxidation primary, secondary or tertiary alcohol | primary only | 108 | |
| 5804564926 | a secondary alcohol creates a ___ under oxidation | ketone | 109 | |
| 5804566672 | a tertiary alcohol creates a ___ under oxidation | nothing | 110 | |
| 5784801942 | glycoside formation | forming acetals or ketals by reactiong hemiacetals or hemiketals with alcohol Hydrolysis rxn (breaks glycosidic bonds) | 111 | |
| 5784806385 | Condensation reaction | forms dissacharides from monosaccharides | 112 | |
| 5784803160 | Sucrose | table sugar alpha-D-glucose + Beta-D-fructose alpha-1,2 glycosidic bond | 113 | |
| 5784803161 | maltose | amylase produces maltose when it breaks down starch alpha-D-glucose + alpha-D-glucose alpha-1,4 glycosidic bond | 114 | |
| 5784803162 | lactose | Beta-D-glucose + Beta-D-galactose Beta-1,4 glycosidic bond | 115 | |
| 5784806716 | cellulose | Beta-D-glucose + Beta-D-glucose Beta-1,4 glycosidic bond | 116 | |
| 5784806809 | starch | alpha-D-glucose + alpha-D-glucose alpha-1,4 glycosidic bond | 117 | |
| 5784808869 | Amylose and amylopectin | how plants store starch | 118 | |
| 5784809528 | alpha amylase beta amylase | cleaves at random spots cleaves at nonreducing end to get maltose | 119 | |
| 5804642846 | liposome | similar to a micelle but is like a circular lipid bilayer | 120 | |
| 5784806880 | glycogen | alpha-D-glucose + alpha-D-glucose alpha-1,4 glycosidic bond every 10th glucose moleucles is has a branched alpha-1,6 glycosidic bond | 121 | |
| 5784808389 | glycogen phosphorylase | cleaves glucose from nonreducing end of glycogen and phosphorylates it to yield glucose-1-phosphate | 122 | |
| 5784810452 | Saturated fatty acids | are solid at room temp, can stack and solidify, more stable ex: butter less fluidity in membranes | 123 | |
| 5804656859 | unsaturated fatty acids | ex: olive oil | 124 | |
| 5784814222 | Glycerophospholipid/phosphoglycerides | All can be categorized as phosphoslipids but not vise versa, it is merely a subgroup of phospholipids Contain a glycerol, 2 FA chains, phosphate and an amino alcohol (that can be neg, pos or neutral) ex: phospatidylcholine, phospatidylethanolamine | 125 | |
| 5784815333 | phosphodiester bond | bond b/w phosphate and sugar | 126 | |
| 5866523467 | anhydride bond | bond b/w phosphates | 127 | |
| 5784815525 | glycosidic bond | bond b/w sphingosine and sugar | 128 | |
| 5784816521 | Sphingolipids | not all are phospholipids (don't contain phosphate) divided into 4 subgroups | 129 | |
| 5784818055 | Glycolipids | contain 2 FA chain, sphingosine, sugar (neutral) not considered phospholipids - no phosphate group, | 130 | |
| 5784818487 | cerebroside | a glycolipid with a single sugar | 131 | |
| 5784818661 | globoside | a glycolipid with two or more sugar | 132 | |
| 5784818834 | ceramide | The simpliest sphingolipid not considered a phospholipid - no phosphate group contain 2 FA chain, sphingosine, H as head group | 133 | |
| 5784818950 | sphingomyelins | are considered phospholipids - contain phosphate group, phosphotidylcholine or phosphotidylethanolamine as head group (neutral) is attached to a phosphate (phoshodiester bond) contain 1 FA chain, sphingosine | 134 | |
| 5784818951 | gangliosides | not considered phospholipids - no phosphate group oligosaccharides with NANA (salic acid) as head groups (negative charge) (glycosidic bond), sphingosine, stearic acid | 135 | |
| 5784820208 | waxes | A fatty acid and secondary or primary long chain alcohol that form esters for protection, water proof | 136 | |
| 5784842205 | terpenes | precursor to steroids built from isoprenes | 137 | |
| 5784842351 | monoterpenes | contain two isoprene units | 138 | |
| 5784842619 | sesquiterpenes | 3 units | 139 | |
| 5784842620 | diterpenes | 4 units vitamin a | 140 | |
| 5784842456 | tripenes | contain six isoprene units make up cholesterol and steroids | 141 | |
| 5784842894 | terpenoids | derived from terpenes precursor to steroids also ex: carotenoids (8 isoprene units) | 142 | |
| 5784843149 | steroids | 4 rings 3 cyclohexane and one cylcopentane ring | 143 | |
| 5804786962 | cholesterol | an amphiphatic molecule that allows membrane fluidity important for bile acids, Vit D, and steroid hormones | 144 | |
| 5804792039 | Cholesterol at low temp | High membrane fluidity | 145 | |
| 5784843615 | prostoglandin | regulates synthesis of cAMP influence sleep/wake, body temp, fever, pain (homeostatic functions ) 20 carbon atoms, including a 5-carbon ring High levels are produced in response to injury or infection and cause inflammation, | 146 | |
| 5784847664 | Fat soluble vitamins | A,D,E,K can't be produced by the body | 147 | |
| 5784847822 | Vitamin A | growth, vision, immune function, and dev. | 148 | |
| 5784847961 | retinal | light sensing molecule | 149 | |
| 5784848049 | retinol | storage form of Vitamin A | 150 | |
| 5784848146 | Vitamin D | food or UV light regulates calcium and phosphate uptake in the intestines which affect bone production | 151 | |
| 5784850496 | Vitamin E | known as tocopherols and tocotrienols in the body (rings in the body that react with free radicals and destroys them thus prevents oxidative damage) are antioxidants | 152 | |
| 5784850497 | Vitamin K | known as phylloquinone and menaquinones in the body helps blood clotting and calcium to bind to proteins forms prothrombin | 153 | |
| 5784851726 | Triglycerides | 3 FA and glycerol primary lipid storage | 154 | |
| 5784852135 | Adipocytes | cells that sore large amounts of fats | 155 | |
| 5784852176 | Saponification | ester hydrolysis of TAGs to make soap with a strong base (NaOH) micelles, like in soap, allow two phases to mix because it turns the hydrophobic ends on the inside and the hydrophilic ends to interact with each other in solution. This is why soap can clean water-soluble (hydrophilic) and non water soluble messes. | 156 | |
| 5807547717 | nucleotides (NDPs, NTPs, NMPs) | base+sugar+phosphate | 157 | |
| 5807547718 | nucleosides | base+sugar | 158 | |
| 5807647204 | Purine bases | two ring structures A and G | 159 | |
| 5807647911 | Pyrimidine | one ring structure T, C and U | 160 | |
| 5807649615 | Aromatic rings | sp2 hybridized are unreactive, very stable | 161 | |
| 5807654239 | Hickels rule | 4n + 2 = pi electrons on aromatic rings | 162 | |
| 5807715940 | Base pair A and T have __ h-bonds | 2 | 163 | |
| 5807715941 | Base pair G and C have __ h-bonds | 3, which make it stronger | 164 | |
| 5807721791 | Chargoffs rule | states that DNA from any cell of all organisms should have a 1:1 ratio (base Pair Rule) of pyrimidine and purine bases and, more specifically, that the amount of guanine is equal to cytosine and the amount of adenine is equal to thymine. | 165 | |
| 5807775105 | Beta-DNA structure | Rt handed helix | 166 | |
| 5807775649 | Z-DNA structure | Lt handed helix, less stable | 167 | |
| 5807777313 | Annealing | forming a double stranded DNA strand | 168 | |
| 5807786610 | PCR | creates copies of DNA strands doubles each round S-eparation of strands using heat A-nnealing primers to attach to templates @ lower temp E-xtention Taq polymerase creates new strand @ high temp | 169 | |
| 5811023404 | PCR enzyme | Ti aquaticus - bacteria enzyme, heat loving | 170 | |
| 5807790273 | nucleosome | a bundle of DNA wrapped in histones only in Eukaryotes Rich in G and C bonds (very stable) | 171 | |
| 5807795302 | Nucloeproteins | proteins are associated with DNA ex: histones | 172 | |
| 5807800525 | heterochromatin | the chromatin in the nucleus that remains tightly coiled during interphase (less likely to be transcribed) appears dark | 173 | |
| 5807802218 | Euchromatin | the chromatin in the cytoplasm that is loosely coiled contains active DNA (the active genes) appears light | 174 | |
| 5807807018 | telomere | the DNA at the end of a chromosome that can't be replicated during DNA replication so it uses an enzyme called telomerases They help to protect chromosomes from unraveling only in Eukaryotes | 175 | |
| 5807815156 | DNA replication in Eukaryotes | single origin of replication two replication forks that move away from each other in opposite directions two identical circular molecules of DNA form | 176 | |
| 5807816582 | DNA replication in Prokaryotes | has multiple origins of replication replication forks move toward each other sister chromatids are created | 177 | |
| 5807834350 | helicase | unwinds the FNA, requires ATP | 178 | |
| 5807844571 | topoisomerase | controls the unwinding and supercoiling works ahead of the helicase and has the opposite effect | 179 | |
| 5807835544 | DNA ligase | forms phosphodiester bonds between the sugar and phosphate joins okazi fragments brings the two strands closer together seals the double helix and seals repairs | 180 | |
| 5807839018 | primase | brings the RNA primer | 181 | |
| 5807839019 | nucleases | enzymes that degrade DNA | 182 | |
| 5807841943 | Single stranded DNA binding proteins | bind to single strands of DNA to prevent binding back to orignal strand and for protection | 183 | |
| 5807965299 | DNA polymerase | synthesizes the new DNA strand in the 5-3 direction reads it in the 3-5 direction it is used on the leading strand | 184 | |
| 5807970105 | The lagging strand | forms small okazi fragments with RNA primers DNA polymerase can fill in the gaps by synthesizing from the 5 end of the RNA primer to the 3 end of another primer More likely to have mistakes bc its made by DNA ligase (no proof reading) | 185 | |
| 5807976007 | Both the leading and lagging strands synthesize __ the replication fork and use RNA primers. Lagging uses __ primer(s) and leadings uses __ primer(s) | toward, many, one | 186 | |
| 5807995931 | After a phosphodiester bond is created using a dNTP, a ___is released | ppi | 187 | |
| 5808003520 | DNA polymerase I (prokayrotes) | removes RNA primers and replaces it with DNA nuceleotides | 188 | |
| 5808005230 | DNA polymerase δ (Eukaryotes) | fills the gap and synthesizes dNTPs when RNA is removed | 189 | |
| 5808010904 | DNA polymerase α, δ and ε (Eukaryotes) | synthesize DNA | 190 | |
| 5808012004 | DNA polymerase γ (Eukaryotes) | replicates mitochondria DNA | 191 | |
| 5808013851 | DNA polymerase β ε (Eukaryotes) | DNA repair | 192 | |
| 5808044356 | DNA polymerase δ ε (Eukaryotes) | for the sliding clamp | 193 | |
| 5808046020 | DNA polymerase III (prokayrotes) | synthesize DNA | 194 | |
| 5808047292 | metastasis | the migration of cancer cells to other tissues | 195 | |
| 5808049266 | oncogenes | mutated genes that cause cancer promote cell cycle | 196 | |
| 5808055787 | tumor suppressor genes or anticogenes | these genes function to inhibit the cell cycle or to stop tumor progression, when mutated, it can't do its job | 197 | |
| 5808075365 | endonuclease | proof reads DNA and removes incorrect bases inside DNA polymerase | 198 | |
| 5808157590 | Which phase in the cell cycle proof reads? | G2 phase | 199 | |
| 5808158922 | Which phase in the cell cycle replicates? | S phase | 200 | |
| 5810956510 | glycosylase enzyme | removes cytosine bases that turn into uracil in DNA and leaves behind a AP site | 201 | |
| 5810971464 | recombinant DNA | molecules are DNA molecules formed by laboratory methods of genetic recombination (cloning) | 202 | |
| 5810978710 | restriction enzymes | recognizes palindromic sequences (the same sequence on strands but in opposite directions) | 203 | |
| 5811034582 | southern blot | uses restriction enzymes to cut and gel electrophoresis to separate DNA fragments into a membrane. The fragment will bind to its complementary sequence and form a double helix. The complementary strand will be labeled to indicate its presence | 204 | |
| 5811048120 | knockout mice | a gene that has been purposely deleted to study a disease | 205 | |
| 5811051262 | transgene | a cloned gene | 206 | |
| 5811053543 | hybridization | joining of complementary base pairs | 207 | |
| 5811261131 | mRNA is created in transcription by | RNA polymerase II binds to DNA at the promotor region (TATA box) and creates an mRNA strand RNA polymerase II also synthesizes snRNA and hnRNA | 208 | |
| 5865929498 | RNA polymerase I | synthesizes rRNA | 209 | |
| 5865932712 | RNA polymerase III | synthesizes tRNA and rRNA | 210 | |
| 5865948173 | Difference between DNA and RNA polymerase | RNA polymerase doesn't need a primer and doesn't proofread | 211 | |
| 5811327525 | mRNA role in translation | contains codons (start AUG) binds to ribosome the codons bind to anticodons brought by tRNA which contains the amino acids takes message from DNA to Ribosome | 212 | |
| 5811351802 | How is translation terminated | when it reaches a stop codon which binds to a release factor | 213 | |
| 5811668448 | tRNA role in translation | aa ataches to 3' end (CCA sequence) brings it to ribosome with mRNA | 214 | |
| 5865967480 | EUK Translation occurs in the | cytoplasm (ribosome) | 215 | |
| 5865972863 | Ribosome binding spots | E(uncharged tRNA leaves) P(grows the poypeptide) A (holds the incoming tRNA) | 216 | |
| 5865987182 | The P site requires what enzyme | peptidyl transferase (forms peptide bonds b/w a.a.) | 217 | |
| 5833173835 | dry ice | solid form of CO2 forms carbonic acid in aqueous solution | 218 | |
| 5833184575 | equilibrium expressions | {Products }/ {Reactants} | 219 | |
| 5833234624 | Enantiomer properties | have the same chemical/physical properties but differ in optical activity to separate: react with a single enantiomer of an optically active compound to form a diasteriomer (have diff chemical/physical properties). Use HPLC after | 220 | |
| 5833259461 | sound waves need a __ to propegate | medium (vacuums don't have a medium) | 221 | |
| 5861343725 | Pyrimidines | are CUT from purines have one ring | 222 | |
| 5861343726 | Purines | contain base pairs A and G (think of as Ag like silver) | 223 | |
| 5865870764 | cDNA libraries | determines mutations by reverse transcribing processed mRNA | 224 | |
| 5865877545 | glycosylation | adds oligosaccharides | 225 | |
| 5866063257 | prenylation | adds lipid group | 226 | |
| 5866205764 | operon | (Prokaryotes) - control gene expression a cluster of genes (that get transcribed together into an mRNA strand) that is controlled by a promoter. Genes in the operon have an 'All or none' expression. can code for enzymes. An operon contains a promotor (where the RNA poly binds), an operator region (where the repressor binds which is encoded by regulatory genes) and a regulatory gene When repressor binds, transcription does not occur bc polymerase is blocked | 227 | |
| 5866240632 | Regulator gene | is a gene involved in controlling the expression of one or more other genes. | 228 | |
| 5866257882 | repressor | a substance that acts on an operon to inhibit messenger RNA synthesis. (prevents transcription) | 229 | |
| 5866249947 | Inducible system | (Prokaryotes) in this process a represser binds to a operator system. It acts as a negative control, to only produce genes when needed. (only does transcription when needed bc it is an energy costly process) ex: lac operon -functions to encode genes to break down lactose by creating lactase. When lactose binds to repressor, the repressor dissociates from the operator region, making those genes available for transcription. Only uses this bacteria when glucose is low, cAMP is produced and binds to CAP. This complex can bind to he promoter region which helps recruit RNA polymerase to transcribe lactase - positive control) (genes are only transcribed in the presence of the specific compound aka lactose) | 230 | |
| 5866249948 | repressible system | in this process the regulatory gene is inactive until it binds to a corepressor. The corepressor binds to the operator site to prevent transcription. ex: trp operon (genes re repressed in the presence of a specific compound and allow for the genes to be turned off) -NEGATIVE FEEDBACK | 231 | |
| 5866300752 | positive control | the binding acts to increase the transcription of a gene | 232 | |
| 5866300753 | negative control | the binding acts to decrease the transcription of a gene | 233 | |
| 5866463519 | Histone acetylase | DNA in histones are more likely to be transcribed becasuse lysine in histone is acetylated (removes the positive charge, decreasing the ineraction between DNA, which is neg charged, and histone) | 234 | |
| 5866477498 | Histone deacetylase | DNA in histones are less likely to be transcribed becasuse acetyl group in histones are removed, silences the gene | 235 | |
| 5866485728 | DNA methylation | DNA is less likely to be transcribed becasuse it adds a methyl group to C and A bases which leads to gene silencing | 236 |
