Consider these three sketches:BAHHHHAAWhich sketches represent the action of an enzyme?Check none of them if none of them do.And finally, for that same sketch, what is C?B|HH|For that same sketch, what is B?Again your answer should be a word or very short phrase.ABIf you said at least one sketch represents the action of an enzyme, for the first sketch that does,what is A?Your answer should be a word or very short (two- or three-word) phrase.3000||33O (none of them)00X

There are three sketches 1, 2 and 3 with labelling A, B and C. We need to identify the enzyme action…

Answered: B A Which sketches represent the action…

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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Similar questions

If you multiplied enzyme concentration by kcat, think about what you would get. Which one of the following would be suitable units? unitless, because the numerator and denominator would both have the same units O s1 M-1 (s) x (M) O Ms
By using Excel or GoogleSheets, graph the Lineweaver-Burk plots for the behavior of an enzyme for which the following experimental data are available. What are the Km and V values for the inhibited and uninhibited reactions? Is the inhibitor competitive or max noncompetitive? [S] (mM) V, No Inhibitor (mmol min-') V, Inhibitor Present (mmol min-') 1× 10-4 5 × 10-4 1.5 × 10-3 2.5 × 10-3 5 × 10-3 0.026 0.092 0.136 0.150 0.010 0.040 0.086 0.120 0.165 0.142 Activate
Is the data that you are collecting in the above table quantitative or qualitative? Explain why. Which treatment had the least amount of browning? Which had the most? Why do you think you obtained these results? Remember that the enzyme polyphenol oxidase is a protein! For each treatment, apply your knowledge of how temperature, pH, and salt concentration affect enzyme activity and explain why you got the results that you did. Include bonds and the levels of protein structure that you explored in Activity A in your answer. How does temperature impact the rate of enzyme activity? If you were to leave the apple in the refrigerator longer, why would it eventually brown? Explain based on what you know about enzyme activity. How does pH and its impact on specific types of bonds explain the results you obtained in your lemon juice treatment? Include bonds and levels of protein structure in your answer. How does salt and its impact on specific types of bonds explain the results you obtained…
The following reactions were catalyzed by an enzyme that follows the Michaelis-Menten mechanism in the absence and presence of inhibitor (10mM). Assume [E]T is the same for each reaction. Determine K, and/or K'. [S] (mM) Uninhibited v (um/s) Inhibited v. (um/s) 1 3 1.67 2 4.5 2.6 6.8 4.5 10 8.1 6.2 20 9.5 7.7
The rate of an enzyme-catalysed reaction was measured in the absence or presence of a non-competitive inhibitor. Which of the following Lineweaver-Burk plots would you expect to see? a. (a) b. (b) c. (c) d. (d)
PA Enzyme (a) Earlier, the activity for this protein/enzyme was tested by monitoring the concentration of the product A' as a function of time. The results are shown in the table below. Copy these numbers into an excel spreadsheet and prepare an enzyme activity plot. Be sure to add all the necessary labels to your plot. (You don't need to copy the plot into this worksheet). Time (min) 0 1 2 3 4 567 A' 8 9 10 11 12 A' (μmol/mL) 0.0 11.0 22.1 33.1 44.1 55.1 66.2 77.2 88.2 92.4 94.5 96.6 96.6 (b) Which part of the data (in minutes) is suitable to use to calculate the activity of the Enzyme, and why? Write downs your answer in the space below.
what is the purpose of staggering the start and stop of the reactions? With reference to your experimental protocol, what is the purpose of staggering the start and stop of the reactions? A.To ensure that the reaction occurs with different amounts of enzyme in each tube so as to ensure comparability between reaction tubes. B.To ensure that the reaction occurs at exactly the same pH in each tube so as to ensure comparability between reaction tubes. C.To ensure that the reaction occurs for exactly the same time interval (30 minutes) in each tube so as to ensure comparability between reaction tubes. D.To ensure that the reaction occurs with exactly the same amount of substrate in each tube so as to ensure comparability between reaction tubes.
You are interested in purifying an enzyme X and decide to use an affinity chromatography followed by an enzymatic assay. You obtain the following data: Total volume of [protein] the sample (ml) (mg/mL) (U) |Total activity Sample name Specific activity |(U/mg) |Affinity | chromatography 2 0.12 5000 20833 You have obtained a 10X fold purification and a yield of 10% at the Affinity step. What was the protein concentration of your crude lysate sample, if its volume was 15 mL? Detail your answer by showing the calculations, and do not forget the UNITS!
Using the appropriate graph and table above, explain what the R48C mutation appears to be doing to the enzyme’s function. Discuss the kinetic parameter changes and their meaning in this context, not the structure of the enzyme, which was not given to you.
The Lineweaver-Burke plot was originally developed in order to "linearize" the data obtained from enzyme kinetics experiments, in order to facilitate the determination of kinetic parameters. Why is it not considered to be an accurate method for this purpose? It is very difficult to draw a straight line on a computer. It is very difficult to calculate the variables required for the "x" and "y" axis. It is more accurate to use the standard "V versus [S]" plot to determine Vmax and KM- The plot weights the least accurate data points the most heavily. It is no longer considered to be acceptable to extrapolate from known data.
A multi-enzyme complex Is made up of three polypeptide chains, A, B and C. A is associated with decarboxylase activity; B is a transacetylase, while C is a dehydrogenase. When the protein was placed in a nonpolar solvent, then run in PAGE, two protein bands were observed. Enzyme assays showed that one protein band exhibited decarboxylase activity while the other has both transacetylase and dehydrogenase activities. When the protein was also placed in an aqueous solvent at pH 5.0, then run in electrophoresis, two protein bands were also detected. Further enzyme assays also showed that one protein band exhibits transacetytase activity while the other has both decarboxylase and dehydrogenase activities. a. What types of non-covalent interactions are possible between A, B and C? b. Addition of urea, a reducing agent gave 4 bands in the PAGE profile with a subsequent loss of decarboxylase activity. What could be the reason for the observed result? Explain briefly in terms of the structure…
A с Wan WWW GHEDE MAK am2 Increasing CE a-1 (no inhibitor) Slope #KY... ...." 7-15 7 a>c²=1 [no inhibitori Slope R 101 9-19 aver-Burk plots in this figure represent the activities of enzymes in the 4-5 n. 155 B D MIN -a'/KM 0.8- 1/V >~- -1/K 0 01 m(app) d'Nmax a=2 a=1.5 1[S] per mM inhibitor a=10 Slope K

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