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- 3. 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).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]8) Indicate which of the five major types of membrane protein (adhesion, enzymatic, recognition, receptor, and transport) is most likely to be involved in each of the situations described below: a) An oncologist wants to study the cells from a certain tumour that has been surgically removed from a patient. However, she must first treat the tumour with a solution affects a membrane protein on the tumour cells. Because of the effect of the solution on the membrane protein, the tumour tissue falls apart into individual cells. Type of membrane protein: b) Farmer Jebediah wakes up in the morning and makes himself an extra-strong coffee. The caffeine in the coffee attaches to a protein in the plasma membrane of his neurons, inducing a signal transduction cascade and causing Farmer Jebediah to be more alert Type of membrane protein:
- All of the following are true of integrins except (a) they are receptor proteins (b) they help organize the cytoskeleton (c) they are part of the ECM (d) they are important in cell signaling (e) they are located in the plasma membraneIf the RGD tripeptide sequence in fibronevtin wete absent. Which is true? integrims would not bind to fibronectin cadherins on adjacent cells would not be able to interact in a homotypic fashion. fibronectin could not form crosslink with other extracellular matrix proteins. glycosaminoglycans would not be able to assemble onto proteoglycans.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
- Drawn below is a schematic of a transmembrane protein. Extracellular Cell membrane Cytosolic side (a) From the list below, select the amino acid(s) that might by more common in the extracellular domain of this membrane protein and whose side- chain can form hydrogen bonds with the surrounding water molecules. Explain why you selected this option(s). Lysine Serine Phenylalanine Methionine (b) From the list below, select the amino acid(s) that would likely be found in the transmembrane/ membrane spanning domain of this protein and whose side- chain interacts with the lipid bilayer. Lysine Serine Phenylalanine MethionineThe transmembrane segments of most integral membrane proteins are made of alpha -helical secondary structures. What is the advantage of this conformation ? How do multiple alpha-helices arrange themselves to form the aqueous pore of an ion channel ?+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.
- 2, Now draw a proposed Glycoprotein involved in cell-cell recognition or signaling embedded in a cell membrane. Draw the glycoprotein with three transmembrane regions. Separately, draw only its primary structure, not embedded in the membrane, with hydrophobic and hydrophilic regions labeled.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)?Look carefully at the transmembrane proteins shown in Figure 11–29. What can you say about their mobility in the membrane?