Campbell Biology
Campbell Biology
12th Edition
ISBN: 9780135188743
Author: Urry
Publisher: PEARSON
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Chapter 11, Problem 7TYU
Summary Introduction

Protein phosphorylation is a post-translational modification (PTM) process. In this process, phosphate groups are added to particular amino acid residues on proteins. This PTM has the potential to alter the stability, subcellular localization, and enzymatic activity of proteins with diverse roles in cells.

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Select statements that accurately describe receptor tyrosine kinases (RTKs). Some RTKs are dimeric in the presence of a ligand. GTPase activity is required for autophosphorylation (cross-phosphorylation). The structure includes a transmembrane helix. The intracellular domain has kinase domains. The a subunit contains seven a helices that span the membrane. A ligand binds to the extracellular domain.
. which of the following statements about heterotrimetric G proteins and their receptors is incorrect? A: when GTP binds to the alpha subunit of the G protein, the beta-gamma subunit dissociates from the alpha subunit B: G-protein coupled receptors contain nine transmembrane alpha helices C: binding of arrestin causes removal of the receptor from the membrane D: G protein- coupled receptors may be desensitized by serine phosphorylation I had chosen option A and got it wrong. What is the Correct answer and explain how it is. Also, where did i go wrong in choosing option A?
Histamine is a chemical substance released in inflammatory and allergic response. The histamine H1 receptor is a G protein-coupled receptor that activates phospholipase C in response to the binding of histamine. Arrange the data below showing the process of histamine signal transduction from the H1 receptor. Calcium ions flow through ligand-gated ion channel. Phosphorylation cascade leads to the activation of a cellular response. Calcioum ions activate a protein, leading to a cellular response. Enzyme cleaves PIP2, forming DAG and IP3. Calcium iom concentration increases in the cytosol. IP3 binds to a ligand-gated ion channel in thw ER membrane.

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Campbell Biology

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