Campbell Biology In Focus, Loose-leaf Edition (3rd Edition)
3rd Edition
ISBN: 9780134895727
Author: Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky
Publisher: PEARSON
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Chapter 4.7, Problem 3CC
MAKE CONNECTIONS The polypeptide chain that makes up a tight junction weaves back and forth through the membrane four times, with two extracellular loops, and one loop plus short C-terminal and N-terminal tails in the cytoplasm. Looking at Figure 3.18, whatWhat would you predict about the amino acids making up the tight junction protein?
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25. Your friend works in a cell biology research lab. She is working
she calls p125, because its molecular mass is 125 kiloDaltons. She knows that
p125 is a transmembrane protein with three membrane-spanning domains. It has
been previously reported that p125 interacts with three other proteins called p175,
p80, and p50 (again,
polyacrylamide gel). These four proteins
in the cell. To determine how these proteins interact with the membrane, you
perform a set of experiments in which you first lyse the cells and save some of
your lysate, which you run in the input lane (labeled "I" in Figure Q25 below).
The lysate is then subjected to a low-speed centrifugation so that you separate out
the membrane fraction (which ends up in the pellet, "P") from the cytoplasm
(which is in the supernatant, "S"). You then wash the pellet from the first
extraction with a high-salt wash that does not disrupt the lipid bilayer, and save a
little bit to run on the gel. After the high-salt wash, you centrifuge…
Match each description with the type of transmembrane protein
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
Methionine
Chapter 4 Solutions
Campbell Biology In Focus, Loose-leaf Edition (3rd Edition)
Ch. 4.1 - Prob. 1CCCh. 4.1 - Prob. 2CCCh. 4.2 - Briefly describe the structure and function of the...Ch. 4.2 - Prob. 2CCCh. 4.3 - What role do ribosomes play in carrying out...Ch. 4.3 - Describe the molecular composition of nucleoli,...Ch. 4.3 - WHAT IF? As a cell begins the process of dividing,...Ch. 4.4 - Describe the structural and functional...Ch. 4.4 - Describe how transport vesicles integrate the...Ch. 4.4 - WHAT IF? Imagine a protein that functions in the...
Ch. 4.5 - Describe two characteristics shared by...Ch. 4.5 - Prob. 2CCCh. 4.5 - Prob. 3CCCh. 4.6 - Prob. 1CCCh. 4.6 - WHAT IF? Males afflicted with Kartageners syndrome...Ch. 4.7 - In what way are the cells of plants and animals...Ch. 4.7 - Prob. 2CCCh. 4.7 - MAKE CONNECTIONS The polypeptide chain that makes...Ch. 4.8 - Colpidium colpoda is a unicellular protist that...Ch. 4 - Which structure is not part of the endomembrane...Ch. 4 - Which structure is common to plant and animal...Ch. 4 - Which of the following is present in a prokaryotic...Ch. 4 - Cyanide binds to at least one molecule involved in...Ch. 4 - Which cell would be best for studying lysosomes?...Ch. 4 - DRAW IT From memory, draw two eukaryotic cells....Ch. 4 - SCIENTIFIC INQUIRY In studying micrographs of an...Ch. 4 - FOCUS ON EVOLUTION Compare different aspects of...Ch. 4 - FOCUS ON ORGANIZATION Considering some of the...Ch. 4 - Prob. 10TYU
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- While investigating structure-function studies in a membrane transport protein, a researcher discovered a single nucleotide mutation that led to the loss of a key alpha-helical segment of the protein in the hydrophilic domain. The mutation that led to this finding is most likely which of the following? Hint: helix breaker O AUC to GUC GAG to CCU GUU to GCU GUG to UUG O CUC to CCCarrow_forwardThe lipid portion of a typical bilayer is about 30 Å thick. (a) Calculate the minimum number of residues in an a-helix required to span this distance. (b) Calculate the minimum number of residues in a B-strand required to span this distance. (c) Explain why a-helices are most commonly observed in transmembrane protein sequences when the distance from one side of a membrane to the other can be spanned by significantly fewer amino acids in a B-strand conformation. (d) The epidermal growth factor receptor has a single transmembrane helix. Find it in this partial sequence: .RGPKIPSIATGMVGALLLLVVALGIGILFMRRRH..arrow_forwardplease help me with this quicklyarrow_forward
- Order following for rate of diffusion through a synthetic lipid bilayer. Explain your order. Cl-, N2, alanine, tRNA, ribose, H2Oarrow_forwardName the three major assumptions made by the "Cell theory". (i) The lipid membrane is composed of lipid molecules. Explain the principle of membrane formation highlighting the role of the physical properties of the lipids. (ii) Comparing dimensions and length scales is often a first step in an analysis. Give an approximate value for the thickness of a lipid bilayer and the linear length of a helical turn of a DNA double helix. A technician wants to amplify DNA from a patient sample. However, the lab is not equipped with a thermocycler. (i) (ii) Name two methods for DNA amplification that can be operated at constant temperature and give their acronyms. Explain these two methods in detail using a schematic and name all necessary components that are required to perform the amplification. Describe the main function of the middle ear. Highlight the role of the ossicles and the tympanic membrane.arrow_forwardUsing the the enzyme acid hydrolase in the lysosome: What is the final destination in which the protein will function? Which features will the protein receive during its manufacture? What is the primary structure (general)? Where is the primary structure made? Where are the secondary and tertiary structures made? Will the protein travel through any organelles during its manufacture? Which ones? What would be the overall result if some part of the manufacture process went wrong, such that the protein ended up as nonfunctional?arrow_forward
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