Terms : Hide Images
| 8335411448 | Universe | The system and its surroundings together. | 0 | |
| 8335411449 | System | All the reactants and products, solvent, and immediate atmosphere >> everything within a defined region of space. | 1 | |
| 8335411450 | Isolated system | If the system exchanges neither matter not energy with its surroundings. | 2 | |
| 8335411451 | Closed system | If the system exchanges energy but not matter with its surroundings. | 3 | |
| 8335411452 | Open system | If system exchanges both energy and matter with its surroundings. | 4 | |
| 8335411453 | Two ways in which living organisms derive energy from their surroundings? | 1. They take up chemical fuels(glucose) from the environment and extract energy by oxidizing them. 2. They absorb energy from sunlight. | 5 | |
| 8335411454 | First law of thermodynamics | In any physical or chemical change, the total amount of energy in the universe remains constant, although the form of the energy may change. | 6 | |
| 8335411455 | Photosynthetic cells | Absorb light energy and use it it to drive electrons from water to carbon dioxide, forming energy-rich products such as glucose, starch, and sucrose. And releasing O2 into the atmosphere. | 7 | |
| 8335411456 | Nonphotosynthetic cells/organisms | Obtain energy by oxidizing the energy-rich products of photosynthesis and then passing electrons to atmospheric O2 to form water, carbon dioxide, and other end products. | 8 | |
| 8335411459 | Potential Energy (energy in cells) | •nutrients in environment •sunlight | 9 | |
| 8335411460 | Cellular work | •chemical synthesis •mechanical work •osmotic and electrical gradients •light production •genetic information transfer | 10 | |
| 8335411461 | Oxidation-reduction reactions | One reactant is oxidized(loses electrons) as another is reduced(gains electrons) | 11 | |
| 8335411462 | Entropy(S) | The randomness or disorder | 12 | |
| 8335411464 | Negative DeltaG | process is spontaneous | 13 | |
| 8335411465 | endergonic reactions | requires energy | 14 | |
| 8335411466 | exergonic reacctions | give off energy | 15 | |
| 8335411467 | Which of the following statements are true about peptide bonds: 1. peptide bonds are amide linkages. 2. peptide bond formation is a hydrolysis reaction. 3. a tetrapeptide contains five amino acid residues. 4. peptides are polymers of proteins. 5. peptide bonds form from ncleophilic attack by an electron pair on an alpha amino nitrogen atom on an alpha caboxyl carbon atom of another amino acid. | 1 and 5. | 16 | |
| 8335411468 | which of the following are functions of amino acids: 1.hormones 2.metabolic intermediates 3. neurotransmitters. 4. carriers of gentetic information. 5. protein components. | 1, 2, 3, 5 | 17 | |
| 8335411469 | glycine | Glycine Gly G Nonpolar |  | 18 |
| 8335411470 | glycine (3 letter) | gly | 19 | |
| 8335411471 | G (1 letter) | G | 20 | |
| 8335411472 | Alanine | Alanine Ala A nonpolar |  | 21 |
| 8335411473 | Alanine (3 letter) | Ala | 22 | |
| 8335411474 | Alanine (1 letter) | A | 23 | |
| 8335411475 | Valine | Valine Val V nonpolar |  | 24 |
| 8335411476 | valine(3 letter) | Val | 25 | |
| 8335411477 | valine (1 letter) | V | 26 | |
| 8335411478 | leucine | leucine leu L nonpolar |  | 27 |
| 8335411479 | leucine 3 | leu | 28 | |
| 8335411480 | leucine 1 | L | 29 | |
| 8335411481 | Isoleucine | isoleucine ILE I nonpolar |  | 30 |
| 8335411482 | isoleucine 3 | ILE | 31 | |
| 8335411483 | isoleucine 1 | I | 32 | |
| 8335411484 | methionine | methionine met m nonpolar |  | 33 |
| 8335411485 | methionine 3 | met | 34 | |
| 8335411486 | methionine 1 | M | 35 | |
| 8335411487 | phenylalanine | phenylalanine phe F aromatic |  | 36 |
| 8335411488 | phenylalanine 3 | PHE | 37 | |
| 8335411489 | phenylalanine 1 | F | 38 | |
| 8335411490 | tyrosin | tyrosine tyr y aromatic |  | 39 |
| 8335411491 | tyrosin 3 | tyr | 40 | |
| 8335411492 | tyrosin 1 | Y | 41 | |
| 8335411493 | tryptophan | tryptophan trp W aromatic |  | 42 |
| 8335411494 | tryptophan 3 | trp | 43 | |
| 8335411495 | tryptophan 1 | W | 44 | |
| 8335411496 | serine | serine ser S polar uncharged |  | 45 |
| 8335411497 | threonine | threonine THR T polar uncharged |  | 46 |
| 8335411498 | threonine 3 | thr | 47 | |
| 8335411499 | threonine 1 | T | 48 | |
| 8335411500 | asparagine | asparagine asn N polar uncharged |  | 49 |
| 8335411501 | asparagine 3 | asn | 50 | |
| 8335411502 | asparagine 1 | N | 51 | |
| 8335411503 | glutamine | glutamine GLN Q polar uncharged |  | 52 |
| 8335411504 | glutamine 3 | GLN | 53 | |
| 8335411505 | glutamine 1 | Q | 54 | |
| 8335411506 | cysteine | cysteine cys C polar uncharged |  | 55 |
| 8335411507 | lysine | lysine lys K polar charged (+) |  | 56 |
| 8335411508 | lysine 3 | lys | 57 | |
| 8335411509 | lysine 1 | K | 58 | |
| 8335411510 | arginine | arginine arg R polar charged (+) |  | 59 |
| 8335411511 | histidine | histidine his H polar charged(+) basic |  | 60 |
| 8335411512 | histidine 3 | his | 61 | |
| 8335411513 | histidine 1 | H | 62 | |
| 8335411514 | glutamic acid | glutamic acid glu E polar charged (-) acidic |  | 63 |
| 8335411515 | glutamic acid 3 | GLU | 64 | |
| 8335411516 | glutamic acid 1 | E | 65 | |
| 8335411517 | Aspartic Acid | Aspartic Acid ASP D polar charged(-) |  | 66 |
| 8335411518 | arpartic acid 3 | ASP | 67 | |
| 8335411519 | aspartic acid 1 | D | 68 | |
| 8335411528 | amino pka | about 9 | 69 | |
| 8335411531 | which of the following statements about amino acids are true: 1.asn and gln are polar amino acids. 2.lysine has one stereocenter. 3.the ala side chain does not form hydrogen bonds with other amino acids. 4.the form of glycine used by the human body is d-glycine. 5.proline has an overall charge at pH seven. 6.phe can undergo oxidation to form tyr. 7.methionine is a thiol. | 1,2,3,6. | 70 | |
| 8335411532 | zwitterion form of an amino acid |  | 71 | |
| 8335411533 | archaea | most inhabit extreme environments | 72 | |
| 8335411534 | bacteria | e coli | 73 | |
| 8335411535 | eukarya | -cells have a nucleus -cells have membrane-bound organelles -many are multicellular -plants -eukaryotes | 74 | |
| 8335411536 | archaea and bacteria | -cells do not have a nucleus -prokaryotes | 75 | |
| 8335411537 | bacteria, eukarya, archae | cells contain genetic material | 76 | |
| 8335411552 | ketone |  | 77 | |
| 8335411557 | carboxyl group |  | 78 | |
| 8335411558 | carbonyl group |  | 79 | |
| 8335411565 | aldehyde |  | 80 | |
| 8335411574 | translation | rna >> protein | 81 | |
| 8335411575 | transcription | dna >> rna | 82 | |
| 8335411576 | reverse transcription | rna >> dna | 83 | |
| 8335411577 | replication | dna >> dna | 84 | |
| 8335411582 | acid | hydrogenated | 85 | |
| 8335411583 | conjugate base | dehydrogenated |  | 86 |
| 8335411585 | titration curve |  | 87 | |
| 8335411586 | pka vs pka relation | whatever has the lower Ka value is favored. | 88 | |
| 8335411588 | how does a buffer resist change in pH upon addition of a stong acid | the stong acid reacts with the weak base in the buffer to form a weak acid, which produces few H+ ions in solution and therefore only a little change in pH. | 89 | |
| 8335411589 | what accurately describes the blood buffering system in humans | bicarbonate buffer system | 90 | |
| 8335411590 | how does hyperventilation affect pH | it decreases CO2 and H+ in the blood, increasing pH. | 91 | |
| 8335411591 | which three of the statements are true: 1. hydrophobic molecules are individually hydrated in water, increasing the entropy of the system. 2. amphipathic(amphiphilic) lipids are the structural basis of biological bilayer membranes. 3. the tendency of water to minimize its contact with nonpolar substances is called the hydrophobic effect. 4. hydrophobic molecules do not readily dissolve in water in part because water molecules involved in hydration cannot participate in normal hydrogen bonding with one another. | 2, 3, 5 | 92 | |
| 8335411602 | Hydrogen bonding | -90% electrostatic in nature -10% quantum mechanical -easily broken and reformed -stronger when in linear formation | 93 | |
| 8335411604 | amphipathic | polar head and nonpolar tail | 94 | |
| 8335411608 | enzymes | biocatalyst enhance the rate of reaction without being consumed by lowering the activation energy. | 95 | |
| 8335411609 | transition state | first the distortion of existing bonds, highest point in reaction diagram | 96 | |
| 8335411610 | activation energy | difference in reactants and transition state | 97 | |
| 8335411611 | catabolism | degradative, free energy yielding reactions | 98 | |
| 8335411612 | anabolism | reactions that require energy | 99 | |
| 8335411613 | metabolism | the overall pathway. | 100 | |
| 8335411614 | deoxyribonucleotides | basic unit of DNA linear polymer of 4 different monomeric subunits | 101 | |
| 8335411615 | native conformation | the precise 3D structure | 102 | |
| 8335411616 | micelles | all hydrophobic groups are sequestered from water. ordered shell of h2O molecules is minimized and entropy is increased. the nonpolar is on the outside. |  | 103 |
| 8335411618 | pH optimum | enyzmes usually show maximum catalytic activity. | 104 | |
| 8336265700 | phosphate buffer system | a reversible reaction that resists pH changes at each pKa that is created by conjugate acid-base equilibrium from the 3 possible hydrogens coming off | 105 | |
| 8336306148 | FRET false negatives | spacial difficulties due to folding (greater than 5nm) or they really don't interact | 106 | |
| 8336350275 | affinity chromatography can separate by what factors? | charge, polarity | 107 | |
| 8336391197 | hydration shell | the hydrogen bonds that form with ions causing salts to dissolve | 108 | |
| 8336415973 | osmolarity | water to solute ratio must be equal in and outside of cells. | 109 | |
| 8336444679 | pH is less than pKa | more acid than base | 110 | |
| 8336456926 | pI | combined pKa, not stable | 111 | |
| 8336464658 | alpha carbon | one carbon from carbon double bonded to O | 112 | |
| 8336494561 | protein-protein interactions | increase entropy, many chemical forces to keep together | 113 | |
| 8336509257 | intracellular buffer | phosphate and histadine | 114 | |
| 8336525005 | spontaneous | don't require energy | 115 | |
| 8336552854 | SDS page | seperation based on size | 116 | |
| 8336562278 | UV spectroscopy | seperation based on aromoticity | 117 | |
| 8336571628 | IEF | seperation based on pI | 118 | |
| 8336579948 | gas chromatography | seperation based on size | 119 | |
| 8336596725 | alpha helix formation | H-bonds in backbone | 120 | |
| 8336608946 | subunit association | R-group to Rgroup or backbone | 121 | |
| 8336639087 | serine protease | break peptide bonds ex trypsin | 122 | |
| 8336702111 | native contact | must be close but not already connected | 123 | |
| 8336729597 | helix-turn helix | DNA binder | 124 | |
| 8336716818 | coiled coil domain | DNA binder | 125 | |
| 8336729598 | BAR domain | homodimer | 126 | |
| 8336789405 | center of membrane residues | hydrophilic | 127 | |
| 8336872786 | liposome | more specific than a pill, a pill can do everything but be as specific | 128 | |
| 8336899529 | Residues most likely to be phosproylated | S, T, Y | 129 | |
| 8336925000 | Prosthetic groups | ions, carbohydrates, cofactors | 130 | |
| 8336941216 | lipid metabolism | high energy release | 131 | |
| 8336947283 | antiport | moves ions in opposite directions | 132 | |
| 8336953936 | symport | moves ions in same direction | 133 | |
| 8336962674 | triglycerides | not in plasma membrane | 134 | |
| 8336980383 | membrane rigidity | impacts the amount of protein protein interactions within the membrane | 135 | |
| 8337004230 | shuttle vectors require | both species origin of rep., restriction sites, selection genes for both species | 136 | |
| 8337027793 | double displacement | ping-pong, AE1 -> XE2 -> BE2-> YE1 | 137 | |
| 8337063446 | single displacement | AEB | 138 | |
| 8337087309 | lysozyme and bacteria | gram positive have peptidoglycan layer which is recognized and broken down by lysozyme. Gram negative is not. | 139 | |
| 8337124467 | alpha linkage | o bond down | 140 | |
| 8337134737 | numbering linkage | same as the carbon numbers that are linked | 141 | |
| 8337153427 | Reducing sugars | have H to give to reduce an oxidant. like in glucose | 142 | |
| 8337255339 | denealing | causes a spike in wavelength at 260nm | 143 | |
| 8337302728 | viability requires | origin of rep but only 1 | 144 | |
| 8337318023 | complementation | reverse and match | 145 | |
| 8337327523 | peptide bonds formed by | ribosomes | 146 | |
| 8337348485 | insertions | don't cut your genes. | 147 | |
| 8337354062 | sanger sequencing | bottom up to 3' | 148 | |
| 8337381724 | pyrosequencing | right to left is 5' to 3' | 149 | |
| 8337431940 | km/ kcat | efficiency, bigger is better | 150 | |
| 8337447761 | Km | constant for enzyme | 151 | |
| 8337460806 | kcat | affinity | 152 | |
| 8337745228 | vmax change | confirmation change, enzyme itself is changed | 153 | |
| 8337768567 | K change | affinity changed | 154 | |
| 8337785076 | competitive inhibition | same binding site | 155 | |
| 8337794082 | noncompetitive inhibition | different binding site | 156 | |
| 8337797246 | allosteric | favors one confirmation over another | 157 | |
| 8337813746 | steady state | the general linear pattern of the M&M graph | 158 | |
| 8337847986 | factor X | clotting by glycosylation of prothrombin to thrombin | 159 | |
| 8337929631 | lower curve | Favors T0 | 160 | |
| 8337945547 | gluconeogenesis | initiated by glycogen phosphorylase in phosphorylated form | 161 | |
| 8337980261 | CAR-T | integrated plasmid with V region and C region | 162 | |
| 8338030529 | Fixing mutations | most specific is Crisper-Cas | 163 | |
| 8338044159 | increase in kM | indicates inhibitor | 164 | |
| 8338059321 | increase vMax | cofactor | 165 | |
| 8338078065 | alphaKG-> glutamate | PPD aminotransferase | 166 | |
| 8338125006 | glutamate with GS | becomes glutamine (gln) | 167 | |
| 8338143388 | pIIa | causes adenylation of GS to turn it off | 168 | |
| 8338149445 | pIId | causes deadenylation of GS to turn it on | 169 | |
| 8338171466 | carbamoyl-P | inhibits glutamine production, made by carbamoyl-p synthetase | 170 | |
| 8338226498 | nucleic acid degradation | produces a lot of Uric acid | 171 | |
| 8338265119 | goal of amino acid degradation | produce 1 of 7 intermediates for energy production | 172 | |
| 8338280291 | R5P-> PRPP | pyrophosphokinase | 173 | |
| 8338302773 | PRPP-> PRamine | amidotransferase | 174 | |
| 8338319339 | IMP | common purine intermediate | 175 | |
| 8338331424 | IMP dehydrogenase | pathway to G | 176 | |
| 8338335837 | adenylosuccinate synthetase | pathway to A | 177 | |
| 8338389155 | UMP | common pyrimidine intermediate | 178 | |
| 8338397616 | CPSII | eukaryotic regulation for pyrimidine synthesis | 179 | |
| 8338410159 | ATCase | prokaryotic regulation for pyrimidine synthesis | 180 | |
| 8338437303 | ribonucleotide reductase | reduces RNA to DNA | 181 | |
| 8338452759 | How many subunits does RNR have | 4 | 182 | |
| 8338456647 | Domains of RNR | A- activation, S- specificity, C-catalytic | 183 | |
| 8338467387 | ATP in S produces | dCTP and dTTP | 184 | |
| 8338489699 | dTTP in S produces | dGTP | 185 | |
| 8338506747 | dGTP in S produces | dADP | 186 | |
| 8338523319 | how to make dTTP | dCDP-> dUMP | 187 | |
| 8338541301 | dCDP-> dUMP | dCMP deaminase | 188 | |
| 8338591834 | EC | energy charge | 189 | |
| 8338594497 | EC of 1 | all ATP | 190 | |
| 8338598431 | EC of 0 | all AMP | 191 | |
| 8338607930 | high EC | favors U reactions | 192 | |
| 8338612679 | U reactions | anabolic, use ATP, like gluconeogenesis | 193 | |
| 8338623865 | R reactions | catabilic, produce ATP like glycolysis | 194 | |
| 8338637911 | brain | most U reactions | 195 | |
| 8338644713 | liver | most R reactions | 196 | |
| 8338694865 | processivity | time from enzyme attaches to when it dissociates | 197 | |
| 8338710156 | Pol1 | medium in all but processivity, has 5'-3' exonuclease, removes primer | 198 | |
| 8338730795 | Pol2 | small in all, but number, for repair | 199 | |
| 8338744710 | Pol3 | biggest in all but number, main replicator | 200 | |
| 8338756056 | all Pol | Mg cofactor | 201 | |
| 8338957937 | Why is RNR a target of cancer drugs? | If you don't have enough dNTPs you cant replicate | 202 | |
| 8338986330 | Mutations | Can cause problems in intron or exon (create alternative splicing) | 203 | |
| 8339032282 | BRACO1 domains | ring finger, BRCT, RAD51 (recombinase) | 204 | |
| 8339063304 | excision | really bad damage is replaced | 205 | |
| 8339080463 | SOS | survival not correct | 206 | |
| 8339086090 | RecBDC | for restarting replication, 1 break, 3' overhang, can have 2 holiday junctions | 207 | |
| 8339133538 | telomere | important for protection | 208 | |
| 8339139694 | cancer | has telomerase, uncontrolled growth, p53 is not active | 209 | |
| 8339169475 | eukaryotes | most regulation of expression | 210 | |
| 8339180049 | capping | guanyly-transferase | 211 | |
| 8339188035 | polyA tail | PAP | 212 | |
| 8339210900 | splicing | intron removed by lariat formed and cut off | 213 | |
| 8339223652 | what removes lariat | transesterifaction | 214 | |
| 8339238539 | interferance | many forms, lncRNA can have multiple functions | 215 | |
| 8339247842 | tRNA | coordination between anticodon and amino acid | 216 | |
| 8339272288 | protein synthesis | ribosome only translates | 217 | |
| 8339282633 | initiation inhibition | eIF2 form a tight complex by phosphorylation | 218 | |
| 8339296691 | regulation of phosphorylation | can be by cofactors or amount of RNA | 219 | |
| 8339330465 | eIF4 | recognizes cap | 220 | |
| 8339334413 | folding process | can be regulated to ensure proper proteins are formed. | 221 | |
| 8339374053 | snap shot | degradation and metabolism are in a ratio at that moment and you can affect one to see the rate of the other | 222 | |
| 8339402893 | misregulations | the opposite of what is supposed to happen | 223 | |
| 8339413207 | glycogen phosphorylase | starts gluconeogenesis | 224 | |
| 8339447135 | gluconeogenesis process regulation | makes glucose or pyruvate is increased in diabetes | 225 | |
| 8339473542 | hemoglobin A1C | amount of glucose bound to hemoglobin | 226 | |
| 8339498720 | Qn site | releases UQ, no electron | 227 | |
| 8339506258 | Qp | releases electron to FeS and UQ to Qn | 228 | |
| 8339531416 | protein kinase | keeps glycolysis going | 229 | |
| 8339540224 | when glucose metabolism is messed up | lipid metabolism increases | 230 | |
| 8339549150 | TPP | made from vitamin B, important cofactor in metabolism | 231 | |
| 8339560090 | lipid metabolism equation | molecules( (cuts+1*10 +cuts (4))-2) | 232 | |
| 8339603831 | pyruvate oxidation | 3 enzymes, 5 cofactors, 1 NADH | 233 | |
| 8339645876 | major minerals | CPPSSCM | 234 | |
| 8339690380 | C4 plants | only have carboxylase in mesophyll cells | 235 | |
| 8339739935 | malate shuttle | NADH to NADH or to citrate or OOA or to CO2 and electron | 236 | |
| 8339766562 | liver PFK | increases gluconeogenesis | 237 | |
| 8339794044 | Treat Diabetes | inhibit glucagon and gluconeogenesis | 238 | |
| 8339832176 | inhibiting gluconeogenesis causes weakness because | turns off pyruvate carboxylase | 239 | |
| 8339850940 | too much ATP | increases glycolysis | 240 | |
| 8339864384 | deficiency in an enzyme | causes all after it to decrease, all before to increase | 241 | |
| 8339898657 | low G6PDH activity | caused by G6P being used for glycolysis, less glucose uptake, and increases ROS | 242 | |
| 8339929372 | cyto C reduction | Complex 3 | 243 | |
| 8339929373 | cyto C oxidation | complex 4 | 244 | |
| 8339943521 | cyanide | complex 3 | 245 | |
| 8339947840 | DCCD | ATP synthase | 246 | |
| 8339956867 | Antimycin | complex 2 | 247 | |
| 8339983112 | demoral | complex1 | 248 | |
| 8340065189 | citrate transport | induces gluconeogenesis | 249 |
