Which phenomenon is not readily explained by the 'induced-fit' hypothesis, that is readily explained bythe 'fluctuation-fit hypothesis?Catalysis by optimal interaction with the transition state of substrates.O Specificity of enzymes for substrates.O Lower binding affinity for products, enabling their release once chemistry has happened.O Cooperativity of binding to the remaining 3 sites of hemoglobin when oxygen binds to the first of the four sites. Below is a figure from the paper on Tar protein being placed into nanodiscs and assayed for biochemicalfunctions (Nanodiscs separate chemoreceptor oligomeric states and reveal their signaling properties. ThomasBoldog. Stephen Grimme, Mingshian Li, Stephen G. Sligar, and Gerald L. Hazelbauer, PNAS August 1, 2006103 (31) 11509-11514; https://doi.org/10.1073/pnas.0604988 103)-R stands for treatment with CheR, an enzyme that methylates the Tar protein on 2 glutamates. CheB isan esterase that can remove methyl groups, but more importantly for this figure, deamidate glutamineto form glutamate. The means no enzyme was added to the Tar protein before it was put in nanodiscsand run on the SDS-PAGE gel. Methylation of the acid group on the glutamate sidechain will remove anegative charge and add mass to the protein. Deamidation changes the mass of glutamine by 1 daltonwhen it forms glutamate, but it adds a negative charge. What can you say about the mobility of themodified proteins compared to the unmodified protein?NanodiscsModification-deamidation- noneamethylation-R BO deamidation makes the protein larger methylation makes it smallerO migration of the bands are accelerated or decelerated opposite to the way expected.their mobilities reflect their mass and charge relative to the unmodified Tar protein

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Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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The above reaction coordinate diagram in the presence of enzyme is inconsistent with the "lock and key" model of enzyme-substrate l binding. Draw and properly label the reaction. coordinate diagram for the enzymatic reaction according to the "lock and key" model. Explain why this model is inconsistent with catalytic properties of enzymes.
Which of the following best indicates a reason why Hisneeds to be a good proton donor (not acceptor) in the catalytic triad mechanism? So that it can create the alkoxide ion. So that it can create a hydroxyde ion. None of the other options is suitable because His's only role is to be a proton acceptor. So that the first product forms and leaves with the correct number of H's. So that it can stabilize the transition state.
The following reaction coordinate diagram charts the energy of a substrate molecule (S) as it passes through a transition state (X‡) on its way to becoming a stable product (P) alone or in the presence of one of two different enzymes (E1 and E2). How does the addition of either enzyme affect the change in Gibbs free energy (ΔG) for the reaction? Which of the two enzymes binds with greater affinity to the substrate? Which enzyme better stabilizes the transition state? Which enzyme functions as a better catalyst?
In a biochemical pathway, three ATP molecules are hydrolyzed. The endergonic reactions in the pathway require a total of 17.3 kcal/mole of energy to drive the reactions of the pathway. What is the overall change in free energy of the biochemical pathway? Is the overall pathway endergonic or exergonic?
Some metabolic enzymes undergo large-scale conformational changes to prevent undesirable sidereactions. Provide one example of an enzyme involved in glycolysis or the citric acid cycle thatundergoes a conformational change upon substrate binding. What is the undesirable side reactionthat the conformational change avoids?
Which of the following is true under the following conditions: an enzyme displaying Michaelis-Menten kinetics where the enzyme concentration is 10 nM, the substrate concentration is 45 mM, and the Km is 50 µM? a) The enzyme has low catalytic efficiency for the substrate. b)The rate of catalysis is near half-maximal velocity. c)The enzymatic reaction is near maximal velocity. d)Halving the substrate concentration has little effect on the catalytic rate. e) There is not enough information provided.
During chymotrypsin-mediated catalysis, which of the following statements is true? Select any/all answers that apply. A. A basic (positively-charged) side chain of the substrate polypeptide sits within the oxyanion hole of the enzyme. B. A basic (positively-charged) side chain of the substrate polypeptide sits within the specificity pocket of the enzyme. C. Ser195 hydrogen-bonds with the backbone carbonyl group of the substrate polypeptide within the oxyanion hole of the enzyme. D. All three residues that comprise the catalytic triad of the enzyme interact directly with the substrate polypeptide chain. E. Both covalent catalysis and acid-base catalysis occur.
a particular enzyme catalyzes a single reactant S to a single product P, following michaelis-menten kinetics rp=(VmaxCs) / (Km + Cs) 1. A reaction with this enzyme is carried out at very low substrate concentrations. Draw and label a curve on the plot that describes the reaction kinetics under those conditions.
When enzyme solutions are heated, there is a progressive loss of catalytic activity over time due to denaturation of the enzyme. A solution of the enzyme hexokinase incubated at 45 °C lost 50% of its activity in 12 min, but when incubated at 45 °C in the presence of a very large concentration of one of its substrates, it lost only 3% of its activity in 12 min. Suggest why thermal denaturation of hexokinase was retarded in the presence of one of its substrates.
Compare and contrast the last three steps of the TCA with the first three steps of β-oxidation. Include relevant chemical structures and reactions. How are these reactions similar in terms of substrates and products, sequence of reactions, involvement of coenzymes? How are they different in terms of fate of the electrons, stereochemistry of the reactants and products…? Compare and contrast the mechanisms of these three steps.
You have been the only one who has been able to this. It has three other parts as well, A) Which Enzyme Catalyzes this reaction? choices are in image provided. B) What is ∆G°' for this reaction? Answer in Joules. K' = 19 C) If the concentration of Glucose-1-phosphate is 48.82 µM at equilibrium, what is the concentration of Glucose-6-phosphate in µM? D) If the reaction is not at equilibrium, what is ∆G' at 25°C if the concentration of Glucose-1-phosphate is 15.04µM and the concentration of Glucose-6-phosphate is 1.62 mM? Answer in Joules. Pay attention to units. Round to the correct number of significant figures. There are 103 µM in 1mM. Thank you and you are the winner for Genius of the day!!
In a Lineweaver-Burk graph, the lines representing the uninhibited and inhibited enzyme catalyzed reaction meet each other on the x-axis. The type of inhibition which is occurring is: a) competitive b) noncompetitive c) uncompetitive d) allosteric CO2 exerts direct activity upon hemoglobin by: a) blocking oxygen from binding to the heme group b) displacing BPG from the central cavity c) oxidizing Fe+2 to Fe+3 which does not bind oxygen d) forming an N-terminal carbamate which favors the T-state The dominant motif found in hemoglobin and myoglobin is: a) helix-turn-helix b) twisted beta sheet c) beta barrel d) random coil Which of these is an ketohexose? a) fructose b) glucose c) ribose d) erythrose Which of these is a constitutional isomer of d-glucose? a) fructose b) galactose c) l-glucose d) ribose Which of these is an enantiomer of d-glucose? a) d-fructose b) d- galactose c) l-glucose d) d-ribose Which of these is a diastereomer of…

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