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Biochemistry Flashcards

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12982027587How do you increase Vmax?The only way is to increase [E]0
12982038109Compare and contrast an MM Enzyme Kinetics plot & the Lineweaver-Burke PlotsIntercepts?1
12982055817what is Km and how can it be used to measure an enzyme's affinity for it's substrate?the concentration of [S] where half the enzyme is filled & a low Km= high affinity and a high Km= low affinity2
12982105249How does competitive inhibition affect Km & Vmax? What does the Lineweaver-Burke Plot look like?Increases Km, Vmax stays the same b/c if we flood a bunch of substrate, can overcome competitors; Lineweaver Burke plot becomes steeper and x-intercept moves toward center3
12982129411How does a noncompetitor affect Km & vmax? Lineweaver-Burke Plot shift?Km is the same because the enzymes that still work retain their same affinity; Vmax is decreased; Lineweaver burke plot becomes steeper. this is when inhibitor binds to the allosteric site4
12982183361What is uncompetitive inhibition? Km & Vmax?inhibitor can only bind to the ES complex; Both Km & Vmax decrease5
12982195882What is the rate determining step?the slowest step in a reaction6
12982203846What Changes During a Phase Changepotential energy & density7
12982213650what level of protein structure is the active site located in?Tertiary structure8
12982224959What are the rate limiting enzymes of glycolysis?Hexokinase (skeletal tissues)/glucokinase (liver/pancreas); PFK-1 (activated by F 2,6, BP through PFK-2); Pyruvate kinase (activated by PFK-1)9
12982247139What are the enzymes in gluconeogensis?Pyruvate carboxylase, PEPCK, F 1, 6 bisphosphatase, Glucose 6 phosphatase10
12982259479What are the rate-limiting enzymes in the citric acid cycle?Isocitrate DH (creates CO2 & NADH); Alpha KG DH (also creates CO2 & NADH)11
12983234277Formula for # of stereoisomers2^n (where n is the # of chiral carbons)12
12983254175(Esp with sugars) enantiomers vs diasteromers?enantiomer= 2 molecules are nonsuperimposable mirror images; diastereomers= molecules are not identical & not mirror images but same connectivity13
12983268551What are epimers?diastereomers that differ at exactly one chiral carbon14
12983337943What are anomers?Differ at the anomeric carbon (vs epimers); alpha anomer= the OH on the anomeric carbon is trans to the CH2OH end; Beta anomer= OH is cis to the CH2OH end15
12983365627What is mutarotation?equilibrium between the α and β anomers.16
12983402625What is a reducing sugar?a reducing sugar is any monosaccharide with a hemiacetal ring17
12983409259Tollen's reagent-detects presence of reducing sugar -uses Ag(NH3)2+ as oxidizing agent *in a + test, aldehydes reduce Ag+ to metallic silver18
12983426291Benedict's reagent-detects presence of reducing sugar -aldehyde group of an aldose is readily oxidized indicated by a red precipitate of Cu2O19
12983459409What is a glycosidic bond?when two monosaccharide rings are bonded using a C-O-C bond; it's a dehydration reaction20
12983678353Which end do you add nucleotide bases to?5'-3' end (add to the 3' end)21
12984538961Glucocorticoids (cortisol)create muscle breakdown22
13082607060What is the Hill coefficient?23
13083812505What is Kcat?- The number of molecules of substrate the enzyme turns into product per unit of time24
13083816191- Km vs Kd- Km can be found at Vmax/2; lower the Km, the higher the affinity - Kd measures the dissociation from the ES complex, so the larger the Kd is, the less affinity the enzyme has to that specific substrate25
13083819867- How does a noncompetitive inhibitor work?- It can bind to either the free enzyme or the ES complex, also considered a mixed inhibitor - No change in Km & decrease in Vmax26
13083822230- How does an uncompetitive inhibitor work?- It can bind to the ES complex - So decreases Vmax, because no matter how much substrate you add, you can't overcome the effects of the inhibitor27
13126618225How does an anion-exchange column work?It pulls anion's down28
13140929687Describe GPCR signalingGPCR's are found in eukaryotic cells & are 7 seven helices transmembrane proteins. When the receptor is inactive, it is bound to a GDP. When a ligand binds to the receptor, it binds to GTP and the receptor has a conformational change. Underneath are 3 subunits. GTP causes the alpha subunit to go off & bind to another protein, which then activates cAMP, which then starts a signal pathway29
13141231013Describe the stages of Non-REMNon-REM: 1) Theta waves (falling asleep) 2) Theta waves (K-complexes and sleep spindles) 3) Delta waves (deep sleep)30
13141388059What brain waves are associated with different levels of consciousness?Beta waves= alertness; alpha waves= light mediation/daydreaming; theta waves= drowsiness & some sleep31
13145427445What is the stability of DNA & RNA dependent on?The number of G-C pairings32
13146788794What kinds of bonds hold together DNA strands?H-bonds33
13160344130Agonist vs. AntagonistAgonist: medication binds to the same site as an endogenous substance (e.g., neurotransmitter) to produce similar response Antagonist: Medication binds to a receptor and thus, prevents the binding and action of an agonist34
13177713808phosphatase vs phosphorylasephosphatases hydrolyze phosphate bonds & release inorganic phosphates; phosphorylases; transfers inorganic phosphates to molecules like AMP35
13188489926endonucleaseAn enzyme that cleaves its nucleic acid substrate at internal sites in the nucleotide sequence.36
13188489927exonucleasean enzyme that removes successive nucleotides from the end of a polynucleotide molecule37
13188492253RibonucleaseNucleic acid digesting enzyme that breaks down ribonucleic acid to produce nucleotides38
13497061693what phosphorylates glucose in the liver? in other organsglucokinase in the liver (hexokinase other places)39
13497720109How many ATP per glucose?about 38 ATP40
13497834777Which e- carriers accept 2 e- while the rest accept 1?flavin rings & ubiquitin41

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