EBK BIOLOGY
4th Edition
ISBN: 8220102797376
Author: BROOKER
Publisher: YUZU
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Chapter 9, Problem 4TY
Summary Introduction
Introduction: The ligand, which is a signaling molecule, shows high degree of specificity towards its receptor. The binding between ligand and receptor occurs when they collide in the correct orientation and form ligand-receptor complex.
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Chapter 9 Solutions
EBK BIOLOGY
Ch. 9.1 - Figure 9.1 Response of a yeast cell to glucose....Ch. 9.1 - Prob. 1BCCh. 9.1 - Which type of signal, paracrine or endocrine, is...Ch. 9.1 - Prob. 3CCCh. 9.2 - Prob. 1BCCh. 9.2 - Prob. 1CCCh. 9.2 - Prob. 2CCCh. 9.3 - Prob. 1BCCh. 9.3 - Prob. 1CCCh. 9.3 - Prob. 2CC
Ch. 9.3 - In the case of signaling pathways involving...Ch. 9.5 - Prob. 1EQCh. 9.5 - Prob. 2EQCh. 9.5 - Prob. 3EQCh. 9.5 - Prob. 1CCCh. 9 - Prob. 1TYCh. 9 - Prob. 2TYCh. 9 - Prob. 3TYCh. 9 - Prob. 4TYCh. 9 - Prob. 5TYCh. 9 - The relay protein Ras is part of the EGF pathway...Ch. 9 - Prob. 7TYCh. 9 - Prob. 8TYCh. 9 - Prob. 9TYCh. 9 - Prob. 10TYCh. 9 - Prob. 1CQCh. 9 - Conceptual Questions What are the three stages of...Ch. 9 - Prob. 3CQCh. 9 - Prob. 1COQCh. 9 - Prob. 2COQ
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- a. Agonist Vs Antagonist b. Receptor Vs enzyme c. Physiologic antagonist Vs inverse agonist d. Facilitated diffusion Vs primary active transport e. Pharmacodynamics Vs Pharmacokinetics Differenciate between them.arrow_forwardProtein A binds to Ligand X with a Kd of 1 μM. Protein B binds to Ligand Y with a Kd of 100 nM. Which of the following statements is TRUE? A. Protein A binds Ligand X ten times tighter than Protein B binds Ligand Y B. At a sufficiently high concentration of ligand, the binding becomes irreversible C. When the concentration of Ligand X is 1 μM, 50% of Protein A is bound to ligand D. Protein B binds to Ligand Y with a Kd of 1 × 10-8 mol/L. E. When both binding reactions are at equilibrium, Protein A has more Ligand X bound than Protein B has ligand Y bound The answer is C, could you show how to get the answer? Thanksarrow_forwardGive detailed Solution with explanationarrow_forward
- Speculate on what the receptor sites for each of these molecules might be in terms of shape and polarity. Suggest an amino acid that could be part of the structure of that receptor site. What is an amino acid that would not line up with the surface properties of each of these compounds (1 for each). (Hint: you can look up the amino acids and their properties. Remember what we’ve talked about in terms of said surface properties and binding).arrow_forwardInteracellular receptors bind a. Hydrophilic molecules B. Cell membrane receptors c. Second messengers such as Camp d. Protein hormones e. Small signals that can diffuse through the cell membranearrow_forwardWhich of the following best describes the type of receptor a beta-antagonist drugs acts on a.Ligand-regulated transmembrane enzymes b.Ion channel c.G protein-coupled receptor d.Intracellular lipid-soluble signalingarrow_forward
- In nerve cells, sodium-potassium pumps exchange two K^++start superscript, plus, end superscript for three Na^++start superscript, plus, end superscript across the cell membrane. What is the primary purpose of this exchange? a.To increase the concentration of K+ outside the cell b.To increase the concentration of K+ outside the cell c.To propagate an action potential d.To increase the concentration of Na+ inside the cellarrow_forwardwhich of the following statements about chemical receptors is correct a. chemical receptors are always found inside the cell b. chemical receptors are always found outside the cell, on the plasma membrane c. chemical receptors are usually lipids d. chemical recetor activity is triggered by agonistsarrow_forwardWhich of the following statements is not true? A. Lidocaine cannot function as a channel blocker if it is not charged B. TTX cannot function as a channel blocker if it is charged C.Lidocaine must fit inside the channel to work as a blocker D.TTX can access its binding site even if the channel is closedarrow_forward
- The 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_forwardWhich of these is not true about the beta-gamma subunit of the heterotrimeric G protein often coupled to 7TM-receptors? Provide explanations for the answers you choose and do not choose. A. it does not change conformations B. when in heterotrimeric form, it increases affinity of alpha subunit for GDP C. it consists of the GTPase domain and the alpha helical domain D. the subunits are bound together by covalently attached lipid moleculesarrow_forwardHormone A binds to its receptor with a KL of 5 μM. In the presence of 2.5 μM compound B and 2.0 μM hormone A, 1.0 μM of A remains unbound. Calculate the binding affi nity of B for the hormone receptor.arrow_forward
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