3. When you think about the primary structure of the mannose-6-P receptor, assuming that it is anintegral membrane protein with one membrane-spanning domain and assuming that it has a ERSS, whatare all of the different protein domains that must be present in this protein's primary structure to get itto where it needs to go and to carry out all of the functions/activities? (Draw a schematic of the proteinstructure/sequence and explain each region).

The internal amino acid sequences in the membrane protein carries the information that determines…

Answered: 3. When you think about the primary…

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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When you think about the primary structure of the mannose-6-P receptor, assuming that it is an integral membrane protein with one membrane-spanning domain and assuming that it has a ERSS, what are all of the different protein domains that must be present in this protein's primary structure to get it to where it needs to go and to carry out all of the functions/activities? (Draw a schematic of the protein structure/sequence and explain each region). What do you think would happen to a soluble protein that normally contains a KDEL tag (ER retrieval) if the tag was cleaved off (where would the protein end up)?
1. The CFTR protein is a chloride channel in the cell membrane. Use your understanding of the biochemical properties/categories of amino acids and how they interact with membrane phospholipids to predict the distribution of charged/polar, and non-polar amino acids within the domains of CFTR listed below. Consider one category to include the charged amino acids and the polar amino acids and the other category to include the non-polar amino acids. For each domain, predict which category of amino acids is likely to be most abundant. Also, explain the rationale behind your prediction. Protein domain Prediction (Charged/Polar or Non-Polar amino acids?) Explanation for prediction TMD1 and TMD2 (transmembrane domains, parts 1-12) ECLs and ICLs (extracellular and intracellular loops) NBD1 and NBD2 R
3. How does dimerization of a receptor tyrosine kinase promotes autophosphorylation of the intracellular domain of the receptor? How does the formation of a dimer helps the phosphorylation reaction?4. Describe where is the phosphate group added on a protein when it gets phosphorylated (what amino acid? what atom?). Then list all the ways that protein function may change after it gets phosphorylated PLEASE ANSWER BOTH
+H₂N-CH-COO™ 1 CH₂ I CH₂ 1 CH₂ I +H₂N-CH₂ A. amino acid D O amino acid B amino acid C O amino acid A +H₂N-CH-COO™ 1 amino acid E C=O B. Of the four amino acids shown, this amino acid would most likely be located in the transmembrane domain of an integral membrane protein. +H₂N-CH-COO™ 1 CH₂ 1 OH C. +H₂N-CH-COO™ I CH H₂C CH₂ D.
1. Integral and peripheral membrane proteins employ multiple strategies to keep them associated to a biological membrane. View these three proteins below, and for each protein shown, answer the following questions: A) What type of membrane protein is this? Integral, peripheral, monotopic, polytopic? How do you know? Justify your label by features of the protein shown in the image. B) Describe the overall tertiary structure of each protein. Be certain to mention hydrophilicity/hydrophobicity of the surfaces of this protein. C) Provide a detailed description of how each protein is held associated to the biological membrane. Protein 2 Protein 3 Protein 1 "H,N. Exterior Cytosol
2. You expressed G-protein coupled receptor T (GPCR T) and reconstituted the receptor in a synthetic phospholipid bilayer. a. Why will you reconstitute the receptor into a lipid bilayer? [2 marks]
6. Define a receptor tyrosine kinase and distinguish it from a serine/threonine kinase. (As we discuss ANY kinase in signalling pathways, pay close attention to what type of kinase it is...does it phosphorylate serene/threonine resides or tyrosine residues?)
Three mechanisms by which membrane-bind-ing proteins bend a membrane are illustrated in FigureQ10–2A, B, and C. As shown, each of these cytosolic mem-brane-bending proteins would induce an invagination ofthe plasma membrane. Could similar kinds of cytosolicproteins induce a protrusion of the plasma membrane(Figure Q10–2D)? Which ones? Explain how they mightwork.
1a-Membrane bound proteins often contain transmembrane domains. These transmembrane domains contain higher amounts of which of the following. Select all that apply. Select one or more: a. Non polar amino acids b. Polar amino acids c.Polar charged amino acids d. Amino acids with hydrophillic residues (R groups) 1b-In most cases, the major function of protein kinases is to: Select one: Oa.Add phosphate groups to certain proteins O b. Hydrolyze GTP to GDP O c. Add CAMP to adenylyl cyclase O d. Facilitate binding of signalling molecules to the associated membrane bound receptor.
Receptor tyrosine kinases such as the epidermal growth factor (EGF) receptor can basically be broken down into three domains: (1) An extracellular, ligand binding domain, (2) A transmembrane domain that must cross through the cell membrane, and (3) an intracellular domain. Match the amino acid with the domain that it would MOST LIKELY be associated with. Lysine (choose (1), (2), or (3) from above) A tyrosine residue capable of being phosphorylated on its hydroxyl group (choose (1), (2), or (3) from above) Isoleucine (choose (1), (2), or (3) from above)
A certain protein is used to activate myosin. If the protein is treated with B-mercaptoethanol, it will not activate myosin. What can you say about the structure of this protein? O The peptide is denatured by B-mercaptoethanol O The peptide does not have a thermodynamically stable configuration O The peptide contains more than one distinct chain O The peptide contains disulfide bonds required for activity
1. Discuss the preferred locations of different classes of amino acids in transmembrane proteins. (Cite sources used)

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