Ter 17°C Question 5 3 Points Consider the reaction progress curves below and complete the following statement by matching each of the blanks (numbered 1-3) with the most appropriate word. (A) Free energy Substrate Product Reaction progress Free energy (B) Substrate Reaction progress Product In reaction (A) the free energy change is BLANK 1 meaning the reaction is BLANK 2 In contrast, reaction (B) can be described as BLANK 3 and not spontaneous. Answers Prompts Select match 1 BLANK 1 Select match (2) BLANK 2 Select match 3 BLANK B Last saved 10:01:55 Questions Filter (16) Q Search K First Last > 館 Continue L P

Ter 17°C Question 5 3 Points Consider the reaction progress curves below and complete the following statement by matching each of the blanks (numbered 1-3) with the most appropriate word. (A) Free energy Substrate Product Reaction progress Free energy (B) Substrate Reaction progress Product In reaction (A) the free energy change is BLANK 1 meaning the reaction is BLANK 2 In contrast, reaction (B) can be described as BLANK 3 and not spontaneous. Answers Prompts Select match 1 BLANK 1 Select match (2) BLANK 2 Select match 3 BLANK B Last saved 10:01:55 Questions Filter (16) Q Search K First Last > 館 Continue L P

Biochemistry

9th Edition

ISBN:9781305961135

Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Chapter15: The Importance Of Energy Changes And Electron Transfer In Metabolism

Section: Chapter Questions

Problem 16RE

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Result nad Discussion Lead Acetate Reaction: Samples: lysine, cysteine, methionine Reagents: 10% Sodium Hydroxide (NaOH) and Lead Acetate Pb(CH3COO)2 -To 1 ml of the amino acid solution taken in a test tube, add few drops of sodium hydroxide (40%) and boil the contents for 5-10 mins over a bunsen burner. Cool the contents and add few drops of 10% Lead acetate solution and observe.
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Part 1: Assess the following partial results section below by editing it for brevity by omitting any unnecessary parts (1 point), explain why you decided to remove certain sections (1 point): To evaluate inhibitory effects of the selected molecules, 10mM stock solutions of each molecule were prepared in DMSO. A reaction mixture (200μl) was prepared with the same formula optimized for the enzyme activity assay (0.1 M Tris-HCl ph 8, 0.1 M KCI, 25 mM NaCl, 0.25 mM ATP, and two units of inorganic yeast pyrophosphatase) with 10 µM of the sample molecule. The reaction mixture was incubated for 20 minutes at ambient temperature. Enzymatic reaction was triggered by addition of the substrate B (0.2 mM) and the absorbance of the product was monitored at 290 nm for 10 minutes. Six out of 15 sample molecules showed appreciable inhibition at 10 μM (Figure 5). Three of the molecules, A3, A6, and A7 exhibited more than 50% inhibition of the enzyme activity and were further diluted to find the minimal…
11) Using the data above, construct Lineweaver-Burk plots. First, graph the inverse of the reaction velocity (rate of reaction) data in column II versus the inverse of the methanol concentration in column I. Then, on the same graph, plot the inverse of the reaction velocity (rate of reaction) data in column III versus the inverse of the methanol concentration in column I
Utilising the provided class data generate the following graphs: I) Michaelis Menten; II) Lineweaver-Burk; and III) Hanes-Woolf. Ensure that you clearly label each graph,and add the relevant trendlines with equations. Table 1: Class data demonstrating the Absorbance at 700nm obtained for the alkaline phosphatase enzyme reaction Table 1 tube Abs700mm 1 0.000 2 0.060 2 0.090 4 0.140 5 0.190 6 0.250 7 0.290 The equipment we used are • 20mM Tris Buffer pH 8.5 • 33mM MgCl2 • Alkaline Phosphatase (2mg/ml) in 20mM Tris Buffer pH 8.5 • 4mM Glucose-1-phosphate • Acid Molybdate pH 5.0 • Reducing Agent • Distilled Water • Glass Test tubes • Tube Rack • Cuvette • Pipettes and Tips • Water bath set to 37oC The method we used is Method/Protocol: 1. Read the protocol in its entirety before starting. Take note of any additional information that appears in subsequent steps that may influence how previous steps are performed. 2. Using glass tubes, generate the reactions mixtures…
Table below shows the kinetic data obtained for an enzyme in the absence of any inhibitor (1), and in the presence of an inhibitor (2), at a concentration of 7.0 mM. Assume the total enzyme concentration, [E]T, is the same for each experiment. Table 1 [S] (mM) Vo Vo {umol/(mL•s)} {umol/(mL•s)} Without Inhibitor With Inhibitor (1) 3.8 (2) 2.2 1 2 7.3 4.3 4 13.3 8.2 8 22.9 14.9 12 30.0 20.4 a); Construct a Lineweaver -Burk plot using the kinetic data shown in Table 1. Determine Vmax and Km for the uninhibited enzyme and inhibited enzyme.
1 pt pt 9146 Bb 9146 Bb 1031 Class Etsy E Traps E Traps New Free Chat + ☆ 出口 keAssignment/takeCovalentActivity.do?locator-assignment-take [References] You do an enzyme kinetic experiment and calculate a Vmax of 118 μmol per minute. If each assay used 0.10 mL of an enzyme solution that had a concentration of 0.20 mg/mL, what would be the turnover number if the enzyme had a molecular weight of 128,000 g/mol? (Enter your answer to two significant figures.) turnover number = sec-1 D 1 pt Submit Answer Try Another Version 2 item attempts remaining estion stion 5 on 6 7 1pt 1 pt 1 pt 1pt 1pt 1pt 1 pt 1 pt D is the substrate concentration multiplied by the catalytic constant. KM is equivalent to the substrate concentration multiplied by the ratio of rate constants for the formation and dissociation of the enzyme-substrate complex. KM is equivalent to the substrate concentration. KM is equivalent to the substrate concentration divided by 2 A: KM is equivalent to the substrate concentration…
Physiology Michaelis Menten relations
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AutoSave 301-Enzyme Kinetics and Inhibition, Part 3 - Compatibility Mode - Word Search ff steve M SM File Home Insert Draw Design Layout References Mailings Review View Help E Share O Comments prepared five different concentrations of substrate (sucrose), and five different concentrations of inhibitor C (plus the control, with zero mM of inhibitor C). The following Table lists the inhibitor C concentrations [I], substrate concentrations [S], and resulting enzyme velocities (V.) for all six of these experiments: [I] O mM O mM O mM O mM O mM [S] Vo 1/[S] 1/ Vo 0.1 mM 0.333333333333 mM per minute 0.2 mM 0.50 0.3 mM 0.60 0.4 mM 0.666666666667 0.5 mM 0.714285714286 0.1 mM 0.1 mM 0.166666666667 0.1 mM 0.2 mM 0.25 0.1 mM 0.3 mM 0.30 0.1 mM 0.4 mM 0.333333333333 0.1 mM 0.5 mM 0.357142857143 0.20 mM 0.1 mM 0.111111111111 0.20 mM 0.2 mM 0.166666666667 0.20 mM 0.3 mM 0.20 0.20 mM 0.4 mM 0.222222222222 0.20 mM 0.5 mM 0.238095238095 0.3 mM 0.1 mM 0.083333333333 0.3 mM 0.2 mM 0.125 0.3 mM 0.3 mM…
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