BIOCHEMISTRY W/1 TERM ACHEIVE ACCESS
9th Edition
ISBN: 9781319425746
Author: BERG
Publisher: MAC HIGHER
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Question
Chapter 10, Problem 14P
Interpretation Introduction
Interpretation:
Whether the concerted model accounts for the given negative cooperativity or not is to be stated.
Concept introduction:
The concerted model suggests that subunits of enzymes are arranged in such connection in which any conformational change in any of the subunit is compulsorily granted to all the subunits.
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Chapter 10 Solutions
BIOCHEMISTRY W/1 TERM ACHEIVE ACCESS
Ch. 10 - Prob. 1PCh. 10 - Prob. 2PCh. 10 - Prob. 3PCh. 10 - Prob. 4PCh. 10 - Prob. 5PCh. 10 - Prob. 6PCh. 10 - Prob. 7PCh. 10 - Prob. 8PCh. 10 - Prob. 9PCh. 10 - Prob. 10P
Ch. 10 - Prob. 11PCh. 10 - Prob. 12PCh. 10 - Prob. 13PCh. 10 - Prob. 14PCh. 10 - Prob. 15PCh. 10 - Prob. 16PCh. 10 - Prob. 17PCh. 10 - Prob. 18PCh. 10 - Prob. 19PCh. 10 - Prob. 20PCh. 10 - Prob. 21PCh. 10 - Prob. 22PCh. 10 - Prob. 23PCh. 10 - Prob. 24PCh. 10 - Prob. 25PCh. 10 - Prob. 26PCh. 10 - Prob. 27PCh. 10 - Prob. 28PCh. 10 - Prob. 29PCh. 10 - Prob. 30PCh. 10 - Prob. 31PCh. 10 - Prob. 32PCh. 10 - Prob. 33PCh. 10 - Prob. 34PCh. 10 - Prob. 35PCh. 10 - Prob. 36PCh. 10 - Prob. 37PCh. 10 - Prob. 38PCh. 10 - Prob. 39PCh. 10 - Prob. 40PCh. 10 - Prob. 41PCh. 10 - Prob. 42PCh. 10 - Prob. 43P
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- need help.arrow_forwardX Incorrect. Suppose that an uncatalyzed reaction is spontaneous because AG has a value of -10 kcal/mol. An enzyme that catalyzes the reaction is identified. What effect will the enzyme have on the rate of the reaction? Choose all that are correct. The enzyme increases the AG value. The enzyme increases the rate of reaction. The enzyme decreases the rate of reaction. The enzyme decreases the AG value. The enzyme raises the activation energy. The enzyme lowers the activation energy.arrow_forwardSelect all that apply. What is true about the conformational aspects of coupling? O The proton gradient is involved in the release of bound ATP from the synthase as a result of conformational change. O The conformational states interconvert as a result of proton flux through the synthase. There are two sites for substrate on the synthase and two possible conformational states: open (0) and tight-binding (T). Dinitrophenol binds to and inhibits ATP synthase conformational changes, thus inhibiting ATP synthesis. The Fo portion of ATP synthase acts as a rotary motor.arrow_forward
- Modified TRUE or FALSE. Write the word TRUE if the statement is correct. If the statement is false, write the incorrect underlined word/s and indicate the correct word/s to make the statement true. The Michaelis-Menten Constant (Km) of an enzyme is equal to the enzyme concentration at which the initial velocity of the reaction is one half of maximum velocity (Vmax).arrow_forwardHand written solutions are strictly prohibited.arrow_forwarddits description. Each term can only be used once. ( Choose] [Choose) on induced fit the free energy of activation, or aclivation energy nds. substrates enzyme-substrate complex on enzyme active site d its description. Each term can only be used once. Chioie pimagepegarrow_forward
- Multiple-Cholce Queations. Read each queation carefully and chooze the beat answer. Enzymes make reactiona go by the activation energy of the теаction. A. alower: ralaing B. fnater: lowering C. faster: raiaing D. alower: lowering What do you call the model which assumes a high degree of recemblance between the shape of the aubatrate & the geometry of the binding site on the enzyme? C. Induced Fit D. Lock and Key A. Van't Hofft B. Michelia-Menten Which of the following does not belong to the group? A. Hydrolasea B. Lipasea C. Lyases D. Transferases Which of the following is true about urease being a hydrolase enzyme? A. It catalyzea the degradation of uracil B. It catalyzes the synthesis C. It catalyzes the hydrolyale of urea D. It catalyzes the degradation of all amines of urea 5. Enzyme are classifed Into how many major groups and ayatematically named by how many numbera separated by dota? A. 4 groups and 6 numbera, гегресtively C. 4 groups and 4 numbera, respectively D. 5 groups and…arrow_forwardModified TRUE or FALSE. Write the word TRUE if the statement is correct. If the statement is false, write the incorrect underlined word/s and indicate the correct word/s to make the statement true. The reaction involving the substrate bound to the active site of an enzyme is made more favorable by increasing the activation energy of the reaction.arrow_forwardnot true about the Michaelis-Menten equation? The equation that gives the rate, v, of an the substrate concentration [S] is the Michaelis-Menten equation = Vmax[S]/(Km + [S]), where V, enzyme-catalyzed reaction for all values of max and Km are constants. Which of the following is a) for [S] << Km, V = Vmax applies to most enzymes, but allosteric enzymes have different kinetics when [S] = Km, then v = Vmax/2 gives the rate when the enzyme concentration, temperature, pH, and ionic strength are constant for very high values of [S], v approaches Vmax e) Which is correct about the constant Km in the Michaelis-Menten equation? also called the catalytic constant or turnover number equal to the number of product molecules produced per unit time when the enzyme is saturated with substrate it is the constant in the first order rate equation v = k[A] it is the constant in the second order rate equation v = equal to the substrate concentration at which the velocity or rate of a reaction is ½ the…arrow_forward
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