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Transcript
ROGUE Biochemistry Jeopardy Find the Penis Sh*t That Came Out of My Mouth I’ve Got 99 Upshots, But a BCH Ain’t One 10 10 10 10 20 20 20 20 20 30 30 30 30 30 40 40 40 40 40 50 50 50 50 50 The BIG Picture I Like Big Bottoms and I cannot Line 10 The BIG Picture – 10 Points 1 ANSWER: L-aspartate 1a ANSWER: L-serine The BIG Picture – 20 Points 2 ANSWER: L-lysine 2a ANSWER: L-histidine The BIG Picture – 30 Points 3 ANSWER: L-leucine 3a ANSWER: L-methionine The BIG Picture – 40 Points 4 ANSWER: L-proline 4a ANSWER: L-asparagine The BIG Picture – 50 Points 5 ANSWER: Beta-sheet 5aa ANSWER: acetylcholine I Like Big Bottoms and I Cannot Line – 10 Points a) A _______________is a graph of the conformational torsion angles phi and psi for the residues in a protein or peptide, a map of the structure of the polypeptide backbone. b) The ____________ approximation postulates that a constant input feed of substrate is supplied whose rate equals that of product formation. c) What chemical group does coenzyme A typically carry in the course of its biochemical function? d) A coenzyme is either a loosely bound cosubstrate or strongly bound ____________. ANSWER: a) Ramachandran plot b) steady state c) acetyl?? d) prosthetic group I Like Big Bottoms and I Cannot Line – 20 Points a) The coenzyme bound carbohydrates UDP-galactose and glucose are required to synthesize __________. b) A _______________ attacks an electropositive site in its role in a chemical (enzymatic) reaction c) A decrease in the activity of an enzyme as a result of binding of a product from the reaction in question or subsequent reactions is referred to as ___________________. d) . The _________________ (or double reciprocal) equation defines parameters that are used to characterize the kinetics of an enzyme. ANSWER: a) lactose b) nucleophile c) feedback inhibition d) Lineweaver-Burk I Like Big Bottoms and I Cannot Line– 30 Points a) The ______________ of an enzymatic catalysis reaction is the rate achieved when it is saturated with substrate. b) What amino acid and functional group in the esterase site of acetylcholine esterase reacts with the substrate? c) The most common amino acid used by enzymes to carry out ____________ is histidine. d) The (vitamin) ________________ is required to synthesize coenzyme NAD+ for use in metabolic redox reactions. ANSWER: a) maximum velocity b) serine hydroxylate c) acid-base catalysis d) niacin I Like Big Bottoms and I Cannot Line – 40 Points a) ____________ functions in transducing the signal of a photon of light into a chemically recognizable form b) Which two amino acids are modified in the reactions catalyzed by cyclin kinase? c) ___________ is the substrate concentration when Vo = Vmax/2. d) The _______________ interaction describes the relation between interatomic distances, electronic charge, solution dielectric and free energies. ANSWER: a) cis-retinal b) tyrosine, threonine c) Michaelis constant d) van der Waals I Like Big Bottoms and I Cannot Line – 50 Points a) (a) Protein _______ structure defines the packing of helices, sheets, turns, etc. (b) Protein primary structure defines the _________. (c) Protein ________ structure defines the relation among subunits in a multisubunit lattice. (d) Protein _________ structure defines the motifs formed by short-range interactions between amino acids. b) Two internal factors that limit the velocity of an enzymatic reaction are _________ and _________. c) A chaotropic agent induces denaturation of proteins by disturbing the ___________________. d) Two examples of irreversible factors that control the catalytic capability of an enzyme are: ______________, ________________ ANSWER: a) (a) tertiary, (b) amino acid sequence, (c) quaternary, (d) secondary b) hydrophobic effect, H-bonding, disulfide bonds, van der Waals forces, ionic bonds (salt bridges) or dipole-dipole interactions c) hydrophobic effect d) covalent modification, proteolysis, irreversible inhibitors Find the Penis – 10 Points DIRECTIONS: Name each structure in order from left to right. ANSWER: glycerol glyceraldehyde glycerate 2,3-bisphosphoglycerate The penis: me Find the Penis – 20 Points DIRECTIONS: Identify each of the following structures: a, b, c, and d. ANSWER: a) activator b) inhibitor c) active site d) allosteric inhibitor site The penis: inhibitor (or most creative) Find the Penis – 30 Points DIRECTIONS: Identify each of the following structures: a, b, c, and d. ANSWER: a) glycogen phosphorylase b b) glycogen phosphorylase kinase c) glycogen phosphorylase a d) glycogen phosphorylase phosphatase The penis: Novice: glycogen phospohorylase, Intermediate: phosphate and arginines, Advanced: same as intermediate but emphasis on “salt bridge” Find the Penis– 40 Points DIRECTIONS: Identify each of the following structures: a, b, c, and d. ANSWER: a) aspartate b) histidine c) serine d) specificity pocket The penis: Awarded based on creativity Find the Penis – 50 Points DIRECTIONS: Identify each of the following structures: a, b, c, and d. ANSWER: a) glutamate b) alpha-ketoglutarate c) oxaloacetate d) aspartate The penis: Awarded based on creativity Sh*t That Came Out of My Mouth– 10 Points a) A _______________ interaction involves polar O, N or both and the atom for which it is named, and constitutes one of the important protein stabilization elements. b) Pyridine aldoximine methiodide (PAM) reactivates __________________, functioning as a nerve gas antidote. c) The coenzyme ____________________________ is required to incorporate the methyl group into thymidine, a necessary prerequisite for the production of DNA. d) Cyclin kinase regulates entry and exit from mitosis by catalyzing a ________ ___________ reaction. ANSWER: a) hydrogen bond b) acetylcholine esterase c) N5,N10-methylenetetrahydrofolate d) covalent modification Double: What pneumonic was used to remember the structure for PAM (draw and explain)! Triple: How are the different hydrogen bond types like relationships Sh*t That Came Out of My Mouth– 20 Points a) An act of catalysis does not change an enzyme and lowers the ___________________ of the associated reaction. b) The catalytic rate constant of an enzyme is abbreviated as _________. c) List the two “chemical modes of catalysis”. d) ___________________ of enzyme catalysis occurs when the inhibitor only binds to the enzyme substrate complex. ANSWER: a) transition state free energy b) kcat c) acid-base, covalent d) Uncompetitive inhibition Double: Transition state free energy was used to describe a real world transition. What was it and how does it demonstrate that women are hateful, hateful liars? Triple: What sexual activity can one get another to do when you reach the substrate concentration required to achieve the maximum initial rate? Sh*t That Came Out of My Mouth– 30 Points a) The most typically cited currency of energy in metabolism is ________________. b) . The _____________ is the characteristic speed of an enzyme’s kinetics extrapolated to the time when a defined amount of substrate is added to the enzyme solution c) A catalytic triad of amino acids is typically present in ______________ . d) The bisubstrate-enzyme ping-pong reaction is used by _____________ in the exchange of an amino group for a carbonyl group between two progressively binding substrates. ANSWER: a)adensoine triphosphate b) initial rate c) serine proteases d) transaminases Double: What is the real-world counterpart of ATP? Triple: In our analogy, what “functional group” is transferred in the ping pong reaction? Quadruple: What is the alt name for the specificity pocket? Sh*t That Came Out of My Mouth– 40 Points a) The other key redox coenzyme is _____________ (not NAD+ or CoQ). b) ___________________ reactions, involving phosphate addition and removal respectively, regulate both glycolysis and the Krebs Cycle. c) Two external factors that limit the velocity of an enzymatic reaction are _________ and _________. d) _________________ of enzyme catalysis occurs when an inhibitor binds to the active site of the enzyme. ANSWER: a) flavin adenine dinucleotide b) Kinase and phosphatase c) pH, solvent polarity, temperature, salt concentration(s) and types, presence of chaotropes, osmolytes d) competitive inhibition Double: What is FAD? Triple: What happens when people are inactive? Quadruple (What!?): What is the scientific name for competitive inhibition? Sh*t That Came Out of My Mouth– 50 Points a) The _____________ noncovalent binding interaction is used to capture ligand-binding entities in the “affinity capture” technique. b) Two examples of reversible factors that control the catalytic capability of an enzyme are: ______________, ________________ c) A zymogen is a protein that is converted from inactive to active forms by a ________________, typically protease cleavage. d) _______________ is used to determine the sequence of a protein based on sequential chemical reactivity. ANSWER: a) biotin-avidin b) noncovalent modifications, pH and pKa changes, [salt] changes, possibly others c) covalent modification d) Edman degradation Double: Draw and describe biotin. Triple: What is the name of my adult club? Quadruple: When in doubt, what do you do to get something off the bead? I Got 99 Upshots, But a BCH Ain’t One – 10 Points a) Our understanding of this function (N5,N10-methylenetetrahydrofolate) can be used in a strategy for (treatment technique) b) The coenzyme _______________ often forms a Schiff base with the alphaamino group of a lysine residue in the enzyme. c) Allosterism involves binding of a regulatory molecule at a site other than the ___________________ d) A/n ________________ works by amplifying an initial signal via several linked protease cleavage reaction stages. (e.g., blood clotting) ANSWER: a) anticancer chemotherapy b) pyridoxal phosphate c) active site d) enzyme cascade I Got 99 Upshots, But a BCH Ain’t One – 20 Points a) A ________________ has two charges which neutralize each other b) A _________________ is the enzyme-substrate combination formed during an enzyme catalysis event c) What kind of reaction produces the reactivated enzyme? d) When ATP used in some biochemical applications it yields AMP and ____________________ ANSWER: a) zwitterion b) Michaelis complex c) nucleophilic substitution d) pyrophosphate I Got 99 Upshots, But a BCH Ain’t One – 30 Points a) The heavy metal _____________ is used to facilitate the biochemical reaction in xanthine oxidase, a key enzyme in purine catabolism. b) List the two “binding modes of catalysis”. c) The Arrhenius equation accounts for the temperature dependence of the ___________. d) Two two examples of irreversible factors that control the catalytic capability of an enzyme are: ______________, ________________ ANSWER: a) molybdenum b) proximity effect, transition state stabilization c) rate of a reaction d) covalent modification, proteolysis, irreversible inhibitors I Got 99 Upshots, But a BCH Ain’t One – 40 Points a) A common process used to produce a nucleophile is: b) _______________ is typically required to achieve optimal activity with (answer 46 “ATP”)-cosubstrate enzyme reactions c) The antibiotic __________________ selectively inhibits cell wall peptidylglycan synthesis in bacteria d) The key polysaccharide in the liver is _________________ ANSWER: a) acid-base catalysis b) Mg +2 c) penicillin d) glycogen I Got 99 Upshots, But a BCH Ain’t One – 50 Points DAILY TRUFFLE