Becker's World of the Cell (9th Edition)
9th Edition
ISBN: 9780321934925
Author: Jeff Hardin, Gregory Paul Bertoni
Publisher: PEARSON
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Textbook Question
Chapter 12, Problem 12.4CC
What features of membrane lipids and proteins contribute to their proper trafficking and targeting in cells?
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Fatty acids must associate with lipid chaperones in order to move within the cell. Why are these chaperones needed, and what is the name given to a group of proteins that are responsible for this intracellular trafficking of fatty acids? What is the key distinguishing feature of these proteins that allows fatty acids to move within the cell?
Gap junctions and tunneling nanotubes are two distinct types of direct intracellular
communication. In comparing and contrasting gap junctions and tunneling
nanotubes, which of the following statements is true?
gap junctions provide a portal for small molecules, proteins and small organelles
to move from cell to cell, tunneling nanotubes only permit small molecules to
pass between cells
typically, there are only two gap junctions that exist between adjacent cells that
are communicating via this mechanism; on the other hand, there are many
tunneling nanotubes between communicating cells
both gap junctions and tunneling nanotubes can pass small molecules between
cells
none of the above is true
Name the three groups into which membrane-associated proteins may be classified. Explain the mechanism by which each group associates with a biomembrane.
Chapter 12 Solutions
Becker's World of the Cell (9th Edition)
Ch. 12 - How do differences in the structure and...Ch. 12 - Why is it necessary for material flowing through...Ch. 12 - What problems would you likely see in cells...Ch. 12 - What features of membrane lipids and proteins...Ch. 12 - Based on what you learned in this chapter about...Ch. 12 - How would an inhibitor of membrane fusion...Ch. 12 - What intracellular transport processes would you...Ch. 12 - What problems would a cell have if it could not...Ch. 12 - Although the plant vacuole resembles the lysosome...Ch. 12 - Why is it important for the biochemical reactions...
Ch. 12 - Compartmentalization of Function. Each of the...Ch. 12 - Endoplasmic Reticulum. For each of the following...Ch. 12 - Biosynthesis of Integral Membrane Proteins. In...Ch. 12 - Coated Vesicles in Intracellular Transport. For...Ch. 12 - QUANTITATIVE Interpreting Data. Each of the...Ch. 12 - Cellular Digestion. For each of the following...Ch. 12 - QUANTITATIVE Virus Entry by Endocytosis....Ch. 12 - Prob. 12.8PSCh. 12 - Sorting Proteins. Specific structural features tag...Ch. 12 - Prob. 12.10PSCh. 12 - Whats Happening? Researchers have discovered a...
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- What TWO factors keep integral trans-membrane proteins embedded firmly within the lipid bilayer?arrow_forwardWhat are integral membrane proteins? Under how many types is it examined? Briefly explainarrow_forwardWhat is the likely identity of these membrane associated proteins: (a) a protein that is released from a membrane treated with a high salt solution, which causes disruption of ionic linkages; (b) a protein that is not released from the membrane upon its exposure to a high salt solution alone, but is released when the membrane is incubated with an enzyme that cleaves phosphate glycerol bonds and covalent linkages are disrupted; (c) a protein that is not released from the membrane upon exposure to a high salt solution, but is released after the addition of the detergent sodium dodecylsulfate (SDS). Will the activity of the protein released in part (c) be preserved following its release?arrow_forward
- Describe two different ways that integral membrane proteins associatewith a membrane. How do peripheral membrane proteins associate witha membrane?arrow_forwardWhat would happen in each of the following cases where something related to intracellular transport is altered? Assume in each case that the protein involved is a soluble protein, not a membrane protein. State where each protein would be located and explain each of your answers. You change the hydrophobic amino acids in an ER signal sequence into negatively charged amino acids. You discover a protein that has both an ER signal sequence and a nuclear localization sequence. The ER signal sequence is at the N-terminus of the protein, and the nuclear localization sequence is located in the middle of the protein.arrow_forwardThe figure above shows the organization of a protein that will eventually reside in the plasma membrane. The boxes labeled 1 and 2 represent membrane-spanning sequences and the arrow represents a site of action of signal peptidase. Which of the following statements must be TRUE about this protein? O a) Most of this protein will project from the cytosolic side of the membrane. O b) The mature version of this protein will span the membrane twice. c) This is a multi-pass membrane protein. O d) The mature version of this protein will span the membrane once.arrow_forward
- What would happen in each of the following cases where something related to intracellular transport is altered? Assume in each case that the protein involved is a soluble protein, not a membrane protein. State where each protein would be located and explain each of your answers. You add a signal sequence (for the Golgi) to the N-terminal end of a normally cytosolic protein. You change the hydrophobic amino acids in an ER signal sequence into other, hydrophobic, amino acids.arrow_forwardProteins may be bound to the exoplasmic or cytosolic face of the plasma membrane by way of covalently attached lip- ids. What are the three types of lipid anchors responsible for tethering proteins to the plasma membrane bilayer? Which type is used by cell surface proteins that face the external medium? By glycosylated proteoglycans?arrow_forwardProteins may be bound to the exoplasmic or cytosolic face of the plasma membrane by way of covalently attached lipids. What are the three types of lipid anchors responsible for tethering proteins to the plasma-membrane bilayer? Which type is used by cell-surface proteins that face the external medium? By glycosylated proteoglycans?arrow_forward
- A transmembrane protein has the following properties: it has two binding sites, one for solute A and one for solute b. The protein can undergo a conformational change to switch between two states: either both binding sites are exposed exclusively on one side of the membrane or both binding sites are exposed exclusively on the other side of the membrane. The protein can switch between the two conformational states only if both binding sites are occupied or if both binding sites are empty, but cannot switch if only one binding site is occupied. What kind of protein do these properties define?arrow_forwardA transmembrane protein has the following properties: it has two binding sites, one for solute A and one for solute b. The protein can undergo a conformational change to switch between two states: either both binding sites are exposed exclusively on one side of the membrane or both binding sites are exposed exclusively on the other side of the membrane. The protein can switch between the two conformational states only if both binding sites are occupied or if both binding sites are empty, but cannot switch if only one binding site is occupied. Do you need to specify any additional properties to turn this protein into a symport that couples the movement of solute A up its concentration gradient to the movement of solute b down its electrochemical gradient?arrow_forwardWhat are the four classifications of membrane proteins? How is each positioned with respect to the bilayer?arrow_forward
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