Campbell Biology: Concepts & Connections (8th Edition)
8th Edition
ISBN: 9780321885326
Author: Jane B. Reece, Martha R. Taylor, Eric J. Simon, Jean L. Dickey, Kelly A. Hogan
Publisher: PEARSON
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Textbook Question
Chapter 5, Problem 12TYK
Sometimes inhibitors can be harmful to a cell; often they are beneficial. Explain.
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Explain how different types of reversible inhibitors can be identified.
In the diagram below, the orange circle represents an effector and the dark purple shapes
(both the diamond and the rod) represent a substrate.
Based on this information, which statement(s) about the diagram is/are true? Select all
that apply.
A
Allosteric
site
B
Allosteric
site
C
Allosteric
site
Allosteric
effector
Active site
Allosteric
effector
Active site,
Allosteric
effector
Novel
binding
site
Rank these substrates in order of best inhibitor (highest binding affinity) to worst inhibitor (lowest binding affinity).
Rank from highest binding affinity to lowest binding affinity. To rank items as equivalent, overlap them.
Chapter 5 Solutions
Campbell Biology: Concepts & Connections (8th Edition)
Ch. 5 - Fill in the following concept map to review the...Ch. 5 - Label the parts of the following diagram...Ch. 5 - Which best describes the structure of a cell...Ch. 5 - Prob. 4TYKCh. 5 - The sodium concentration in a cell is 10 times...Ch. 5 - The synthesis of ATP from ADP and a. stores energy...Ch. 5 - Facilitated diffusion across a membrane requires...Ch. 5 - What are the main types of cellular work? How does...Ch. 5 - Why is the barrier of the activation energy...Ch. 5 - Relate the laws of thermodynamics to living...
Ch. 5 - How do the components and structure of cell...Ch. 5 - Sometimes inhibitors can be harmful to a cell;...Ch. 5 - Cells lining kidney tubules function in the...Ch. 5 - SCIENTIFIC THINKING Mercury is known to inhibit...Ch. 5 - A biologist performed two series of experiments on...Ch. 5 - Organophosphates (organic compounds containing...
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- The biomolecular interaction between protein receptors and ligands is similar to that of en- zymes and substrates, which depends in part on the shape of the protein. The shape of a protein, in turn, depends on the presence of appropriate chemical bonds in the protein. Many common medications function by altering the interactions between protein receptors and ligands, thereby interfering with the normal response of a cell to specific signals. Which of the following best describes a mechanism by which a drug might interfere with a normal cellular response? A B A medication causes the cell to become more permeable and unable to maintain the conditions that allow a normal response. с A medication interrupts the electron transport chain in a cell and makes it unable to syn- thesize sufficient ATP. D A medication enters the nucleus of a cell and alters the nucleic sequence for a specific receptor protein. A medication enters a target cell and acts as an inhibitor to an intercellular protein…arrow_forwardChoose (+) if the following circumstances or situations will most likely result to production of intrinsic activity; if otherwise, choose (-)arrow_forwardDiscuss the physiological applications of colligative properties.arrow_forward
- Draw and label the Lineweaver–Burk, Plots for each type of inhibitor.arrow_forwardKinases, in general, are enzymes that Question 8 options: A) are always covalent modification, inhibitors. B) do not alter target activity. C) add phosphate groups to usually serine, tyrosine, or threonine. D) remove phosphate groups from serine, tyrosine, or threonine. E) all of the abovearrow_forwardIncreasing the number of inhibitors will increase the overall rate of the reaction. True or falsearrow_forward
- Which of the following protein domains would you expect to find in an "easily druggable" target but NOT in an "undruggable" target. An easily druggable target is defined as a target with an easily accessible active site than can be activated or inhibited. Please Explain. Answer Choices: A) Extracellular domain B) Intracellular domain C) Membrane Spanning domain D) ATP-binding domain E) Protein Binding domainarrow_forwardOne way of identifying a drug target in a complex cellular extract is to use an affinity approach, i.e. fix the drug to a resin (agarose etc) and use it to "pull down "" the target from the extract. What potential problems do you think may be encountered with attempting this approach?arrow_forwardThe Graph below shows the binding curves of two proteins (A and B) for the same ligand (L). Use this Graph and determine the dissociation constant, K, for both proteins. Which protein (A or B) has a greater affinity for ligand L? Which of the two proteins would be more easily inhibited by an antagonist? 1.0 Y 0.5 2 A 4 6 B 8 [L] (μM) 10 12 14 16arrow_forward
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