Discuss reuptake and enzymatic degradation (breakdown) in the context of the appropriate neurotransmitters. Please include peer reviewed references.
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Discuss reuptake and enzymatic degradation (breakdown) in the context of the appropriate neurotransmitters. Please include peer reviewed references.
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- Starting from the situation below, explain the next immediate steps that occur after the agonist ligand binds to the GPCR. Describe what happens in terms of the GTP and the heterotrimeric G protein structure. www www Ligand α В GTP ZAN Y Copyright ©2009 Pearson Education, Inc. GDPInhibitors of acetylcholinesterase, such as edrophonium, are used to treat Alzheimer’s disease. The substrate for acetylcholinesterase is acetylcholine. Structures are attached. What kind of inhibitor is edrophonium? Explain. Can inhibition by edrophonium be overcome in vitro by increasing the substrate concentration? Explain. Does this inhibitor bind reversibly or irreversibly to the enzyme? Explain.Can you please describe the role of G proteins in ligand-activated cellular signal transduction.
- Please asapPls provide side by side difference of the steps in the synthesis of catecholamines and acetylcholine.Describe the general function and structural features of G-protein-coupled receptors (GPCRs). Be sure to include an explanation of GTPase activating proteins (GAPs) and GDP exchange factors (GEFs) in the context of the GTPase cycle. How are different classes of heterotrimeric G-proteins defined?
- . Based on what you know about enzyme inhibition, classify the following examples as irreversible, competitive, or noncompetitive enzyme inhibition. A) competitive B) noncompetitive C) irreversible 1) Diisopropyl fluorophosphate binds to acetylcholinesterase and permanently inactivates the enzyme. Paralysis results. 2) A drug binds to the active site of an enzyme but disassociates and leaves the enzyme active. 3) A toxin binds to the surface of an enzyme. The enzyme then binds the substrate, but no product is produced. The toxin may disassociate and the enzyme will become active again. 4) Vitamin K is a coenzyme involved in blood clotting. An anticoagulant drug binds at the site of vitamin K bonding, blocking vitamin K binding and preventing clotting. Clotting resumes after the patient stops taking the drug. 5) Aspirin binds to prostaglandin synthetase and permanently stops its ability to produce prostaglandin.Activation of phosphatidylinositol-3-kinase (PI3K) stimulate protein-protein interactions. True or FalseLigand binding to proteins may occur with varying strengths; some ligands bind tightly to proteins while others bind less tightly. The strengths of reversible binding are determined experimentally by varying concentrations of ligands, and measuring the saturation of the protein in the various ligand concentrations. One such laboratory study investigated the binding of a hormone to three different receptor proteins in the cell membrane. The data collected are shown in the table below: 1) Provide a brief explanation as to why ligand binding to proteins must be a reversible process. 2) Calculate the dissociation constant (Kd) for the hormone binding to each of the three proteins.