Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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Question
Chapter 15, Problem 38P
Interpretation Introduction
Interpretation:
The processes that take place in the living organisms which need a constant input of free energy are to be stated.
Concept introduction:
A group of
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Compare and contrast primary and secondary active transport mechanisms in terms of energy utilisation and efficiency. Provide examples of each and discuss their physiological significance in maintaining ionic balance and nutrient uptake.
Rubric
Understanding the key concepts (clearly and accurately explains primary and secondary active transport mechanisms, showing a deep understanding of their roles)
Energy utilisation analysis ( thoroughly compares energy utilisation in primary and secondary transport with specific and relevant examples
Efficiency discussion
Use of examples (provides relevant and accurate examples (e.g sodium potassium pump, SGLT1) with clear links to physiological significance.
Clarity and structure (presents ideas logically and cohesively with clear organisation and smooth transition between sections)
9. Which one of the compounds below is the major organic product obtained from
the following reaction sequence, starting with ethyl acetoacetate?
요요.
1. NaOCH2CH3
CH3CH2OH
1. NaOH, H₂O
2. H3O+
3. A
OCH2CH3
2.
ethyl acetoacetate
ii
A
3. H3O+
OH
B
C
D
E
7. Only one of the following ketones cannot be made via an acetoacetic ester
synthesis. Which one is it?
Ph
کہ
A
B
C
D
E
Chapter 15 Solutions
Biochemistry
Ch. 15 - Prob. 1PCh. 15 - Prob. 2PCh. 15 - Prob. 3PCh. 15 - Prob. 4PCh. 15 - Prob. 5PCh. 15 - Prob. 6PCh. 15 - Prob. 7PCh. 15 - Prob. 8PCh. 15 - Prob. 9PCh. 15 - Prob. 10P
Ch. 15 - Prob. 11PCh. 15 - Prob. 12PCh. 15 - Prob. 13PCh. 15 - Prob. 14PCh. 15 - Prob. 15PCh. 15 - Prob. 16PCh. 15 - Prob. 17PCh. 15 - Prob. 18PCh. 15 - Prob. 19PCh. 15 - Prob. 20PCh. 15 - Prob. 21PCh. 15 - Prob. 22PCh. 15 - Prob. 23PCh. 15 - Prob. 24PCh. 15 - Prob. 25PCh. 15 - Prob. 26PCh. 15 - Prob. 27PCh. 15 - Prob. 28PCh. 15 - Prob. 29PCh. 15 - Prob. 30PCh. 15 - Prob. 31PCh. 15 - Prob. 32PCh. 15 - Prob. 33PCh. 15 - Prob. 34PCh. 15 - Prob. 35PCh. 15 - Prob. 36PCh. 15 - Prob. 37PCh. 15 - Prob. 38PCh. 15 - Prob. 39P
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- Four distinct classes of interactions (inter and intramolecular forces) contribute to a protein's tertiary and quaternary structures. Name the interaction then describe the amino acids that can form this type of interaction. Draw and annotate a diagram of the interaction between two amino acids.arrow_forwardExamine the metabolic pathway. The enzymes that catalyze each step are identified as "e" with a numeric subscript. e₁ e3 e4 A B с 1° B' 02 e5 e6 e7 E F Which enzymes catalyze irreversible reactions? ப e ez ☐ ez e4 ☐ ப es 26 5 e7 Which of the enzymes is likely to be the allosteric enzyme that controls the synthesis of G? €2 ез e4 es 26 5 e7arrow_forwardAn allosteric enzyme that follows the concerted model has an allosteric coefficient (T/R) of 300 in the absence of substrate. Suppose that a mutation reversed the ratio. Select the effects this mutation will have on the relationship between the rate of the reaction (V) and substrate concentration, [S]. ㅁㅁㅁ The enzyme would likely follow Michaelis-Menten kinetics. The plot of V versus [S] would be sigmoidal. The enzyme would mostly be in the T form. The plot of V versus [S] would be hyperbolic. The enzyme would be more active.arrow_forward
- Penicillin is hydrolyzed and thereby rendered inactive by penicillinase (also known as ẞ-lactamase), an enzyme present in some penicillin-resistant bacteria. The mass of this enzyme in Staphylococcus aureus is 29.6 kDa. The amount of penicillin hydrolyzed in 1 minute in a 10.0 mL. solution containing 1.00 x 10 g of purified penicillinase was measured as a function of the concentration of penicillin. Assume that the concentration of penicillin does not change appreciably during the assay. Plots of V versus [S] and 1/V versus 1/[S] for these data are shown. Vo (* 10 M minute"¹) 7.0 6.0 5.0 4.0 3.0 20 1.0 0.0 о 10 20 30 1/Vo (* 10 M1 minute) 20 103 90 BO 70 50 [S] (* 100 M) 40 50 60 y=762x+1.46 × 10" [Penicillin] (M) Amount hydrolyzed (uM) 1 0.11 3 0.25 5 0.34 10 0.45 30 0.58 50 0.61arrow_forwardConsider the four graphs shown. In each graph, the solid blue curve represents the unmodified allosteric enzyme and the dashed green curve represents the enzyme in the presence of the effector. Identify which graphs correctly illustrate the effect of a negative modifier (allosteric inhibitor) and a positive modifier (allosteric activator) on the velocity curve of an allosteric enzyme. Place the correct graph in the set of axes for each type of modifier. Negative modifier Reaction velocity - Positive modifier Substrate concentration - Reaction velocity →→→→ Substrate concentration Answer Bankarrow_forwardConsider the reaction: phosphoglucoisomerase Glucose 6-phosphate: glucose 1-phosphate After reactant and product were mixed and allowed to reach at 25 °C, the concentration of each compound at equilibrium was measured: [Glucose 1-phosphate] = 0.01 M [Glucose 6-phosphate] = 0.19 M Calculate Keq and AG°'. Код .0526 Incorrect Answer 7.30 AG°' kJ mol-1 Incorrect Answerarrow_forward
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