Choose from the dropdown menu, the description that best matches each of the components shown. A se C V [ Select ] A: multipass transmembrane protein phospholipid polar heads single pass transmembrane protein B: peripheral membrane protein lipid-anchored protein C: [ Select ] D: [ Select ] E: [ Select ]
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- 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 MethionineHow long is a typical transmembrane domain, and what is the chemical composition of the amino acids found within the transmembrane domain of a single-spanning integral membrane protein? A~ 20 amino acids; hydrophobic amino acidsB~ 100 amino acids, amphipathic amino acidsC~ 10 amino acids; polar, charged amino acids D~ 50 amino acids, polar, uncharged amino acidsList 2 functions of peripheral membrane proteins
- List 2 functions of peripheral membrane proteinYou will create a hand drawn, 2-dimensional, labelled diagram of the plasma membrane (not a 3D diagram). Label the following structures in your diagram: A phospholipid A peripheral protein An integral protein A cholesterol Intracellular and extracellular portion of the membrane Hydrophobic and hydrophilic areas Also include a detailed drawing of a single phospholipid labeling its componentLook carefully at the transmembrane proteins shown in Figure 11–29. What can you say about their mobility in the membrane?
- Focal adhesion complex attachment to extracellular matrix molecules is mediated by: heterodimers of alpha-integrin and beta integrin homodimers of classical cafherins The force of gravity actin filamentsYou are using fluorescence microscopy to study a plasma membrane protein that is fused to green fluorescent protein (GFP). Adding GFP to a protein allows us to monitor the protein in live cells using light microscopy without the need for any special stains. Under baseline conditions, the fusion protein is evenly distributed over the surface of the cell. You use the microscope software and laser to photobleach an ROI and watch for the recovery of fluorescence in real time. you have a control protein, a GFP fusion with the insulin receptor, where the ROI fully recovers from photobleaching in 10 min. However, when Protein X is fused with GFP, the fluorescence recovers only to 10% the starting levels in 10 min in the same cell type under the same experimental conditions. Provide two different, reasonable explanations for the different results with these two fusion proteins.When rhodamine-dyed mouse proteins were first mixed with fluorescein-dyed human proteins (in mouse/human hybrid cell fusions), these proteins appeared to exhibit: restricted movement, based on confinement by diffusion barriers restricted movement, based on tethering to extracellular molecules unrestricted movement, similar to membrane phospholipids restricted movement, based on anchoring to intracellular proteins restricted movement, based on attachment to other cells
- n addition to transmembrane a-helices another type of polypeptide structure of Integral membrane proteins that extends through the lipid bilayer is: segments with mainly charged amino acids B barrel segments with mainly polar amino acids single B-strand irregular secondary structure d)In an integral membrane protein, which of the amino acids below is most likely to be found in the interfacial region of the bilayer? Group of answer choices Lys Ala Phe LeuDraw a lipid bilayer, and focus on three lipids that are on the same side of the membrane. Color in the areas where you expect the hydrophobic interactions, and in another color, shade in the areas that are hydrophilic. Draw another lipid bilayer, and for this one, include two membrane proteins. One of them should be an integral membrane protein and the other one a peripheral membrane protein. Label the lipid bilayer, the side the faces the cytoplasm and the side that faces outside the cell. Also label the two proteins, and shade in the areas where you predict that you would find hydrophobic amino acids and hydrophilic amino acids.