Study Guide for Campbell Biology
11th Edition
ISBN: 9780134443775
Author: Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Jane B. Reece, Martha R. Taylor, Michael A. Pollock
Publisher: PEARSON
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Chapter 7, Problem 3TYK
Summary Introduction
Introduction: Integral membrane proteins are a type of membrane proteins that are firmly bound to the membrane. These types of proteins are amphipathic in nature. Their hydrophilic head region is extended out of the cell, and its hydrophobic tail region interacts with the fatty acids present on the membrane phospholipids.
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Students have asked these similar questions
why do transmembrane proteins cross the phospholipid bilayer as an a-helix or B-barrel?
A. These structures arrange polar peptide bonds and hydrogen bonds to the exterior of the helix or barrel while nonpolar side chains are on the interior.
B. These structures sequester polar peptide bonds and hydrogen bonds to the interior of the helix or barrel
while nonpolar sidechains are on the exterior.
The plasma membrane of E. coli is about 75% protein and 25% phospholipid by weight. How many molecules of membrane lipid are present for each molecule of membrane protein? Assume an average protein Mr of 50,000and an average phospholipid Mr of 750. What more would you need to know to estimate the fraction of the membrane surface that is covered by lipids?
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amino acid D
O amino acid B
amino acid C
O amino acid A
+H₂N-CH-COO™
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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™
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CH₂
1
OH
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+H₂N-CH-COO™
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Chapter 7 Solutions
Study Guide for Campbell Biology
Ch. 7 - Label the components in the following diagram of a...Ch. 7 - a. Cite some experimental evidence that indicates...Ch. 7 - List the six major functions that membrane...Ch. 7 - What types of molecules have difficulty crossing...Ch. 7 - A solution of 1 M glucose is separated by a...Ch. 7 - a. What osmotic problems does the freshwater...Ch. 7 - Prob. 7IQCh. 7 - Prob. 8IQCh. 7 - a. How is cholesterol transported into human...Ch. 7 - Create a concept map to illustrate your...
Ch. 7 - The following diagram illustrates passive and...Ch. 7 - If a single layer of phospholipids coats the water...Ch. 7 - Glycoproteins and glycolipids are important for a....Ch. 7 - Prob. 3TYKCh. 7 - Prob. 4TYKCh. 7 - Prob. 5TYKCh. 7 - Use the following U-tube setup to answer questions...Ch. 7 - Use the following U-tube setup to answer questions...Ch. 7 - Use the following U-tube setup to answer questions...Ch. 7 - How much work is expended in diffusion? a. an...Ch. 7 - Prob. 10TYKCh. 7 - Prob. 11TYKCh. 7 - Water passes quickly through cell membranes...Ch. 7 - Facilitated diffusion of ions across a cellular...Ch. 7 - Prob. 14TYKCh. 7 - Which of the following describes cotransport? a....Ch. 7 - Prob. 16TYKCh. 7 - An animal cell moves potassium against its...Ch. 7 - Prob. 18TYKCh. 7 - Prob. 19TYKCh. 7 - In response to low blood pressure, the adrenal...
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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 Methioninearrow_forward1. 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 Cytosolarrow_forwardSequence analysis of a membrane protein shows four 20-amino acid long stretches of residues that are predominantly hydrophobic. Between each of these stretches of hydrodophobic residues, a stretch of predominantly hydrophilic residues is found. From this observation one can reasonably postulate that: A. this is a peripheral membrane protein which interacts with the membrane via hydrophobic interactions B. this protein has 4 alpha helical segments that span the membrane C. this protein can be removed from the membrane by dramatically increasing the salt concentration. D. this is a 4 stranded beta barrel which spans the membrane E. this is a glycoprotein Facilitated diffusion (passive transport) through a biological membrane is A. driven by a concentration gradient. B. generally irreversible. C. endergonic. D. driven by the ATP to ADP conversionarrow_forward
- Sequence analysis of a membrane protein shows four 20-amino acid long stretches of residues that are predominantly hydrophobic. Between each of these stretches of hydrodophobic residues, a stretch of predominantly hydrophilic residues is found. From this observation one can reasonably postulate that: A. this is a peripheral membrane protein which interacts with the membrane via hydrophobic interactions B. this protein has 4 alpha helical segments that span the membrane C. this protein can be removed from the membrane by dramatically increasing the salt concentration. D. this is a 4 stranded beta barrel which spans the membrane E. this is a glycoproteinarrow_forwardChoose the statements that describe how the helix orients in the tertiary structure of an integral membrane protein. The threonine residues act as membrane interface anchors, interacting with the lipid bilayer and the aqueous environment. The amphipathic helix interacts with the lipid bilayer along its hydrophobic surface, exposing its hydrophilic surface to the aqueous environment. A group of helices cluster with their polar surfaces in contact with one another and their hydrophobic surfaces facing the lipid bilayer. The peptide entirely embeds in the lipid bilayer. Incorrectarrow_forwardDrawn below is a schematic of a transmembrane protein. Extracellular Cell membrane Cytosolic side (a) When this transmembrane protein is embedded in the lipid bilayer, what is the highest order of structure (choose from primary, secondary, tertiary and quaternary) of this protein? Explain why you selected this option.arrow_forward
- A researcher is isolating proteins from a cell via different techniques. They find that when the cell is ground with a blender, all of the proteins in the cell can be extracted. However if instead the cell membranes are agitated in a 1.2 M KCl mixture, only about 70% of the total protein is extracted.What class of membrane proteins are in this soluble extract and what forces normally hold them to the membrane?What class of membrane proteins are the 30% of proteins that remain behind, and what forces hold these proteins in the membrane? If a solution of ionic solids was not available, what other solvent systems could be used to extract these proteins?arrow_forwardIon channels are formed by a particular kind of membrane protein that allows the passage of a specific ion (or ions) under certain conditions. This type of protein is most likely a(n) a. peripheral membrane protein with additional hydrophobic domains b. integral membrane protein with a transmembrane domain c. a cholesterol-like molecule that is positioned in the phospholipid bilayer d. membrane phospholipid with hydrophilic head group e. soluble enzyme anchored to a scaffolding protein on the cytoplasmic side of the plasma membranearrow_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_forward
- In the figure below, an integral membrane protein is shown. These proteins sit inside of cell membranes. Some integral proteins are membrane channels or transporters, while others serve as enzymes, receptors, or anchors. Describe the differences you would expect to see in the amino acid side chains on the outer surface of an integral cell membrane protein, as compared to a water-soluble globular protein. Be sure to discuss the chemical nature of the cell membrane in your answer.arrow_forwardMany transmembrane proteins are oligomeric, with several identical subunits. The oligonmers are usually found to have some form of C, symmetry, rather than D, or any higher order. Suggest a reason for this observation.arrow_forward1. Researchers have discovered a new membrane protein that has three transmembrane domain αhelixes that span the lipid bilayer. a. If the lipid bilayer is 30 Å thick, what is the smallest number of amino acid residues that can be in each α-helixes for them to be long enough to span the bilayer? b. If one of the three α-helixes is titled at a 32° angle relative to an axis perpendicular to the surface of the lipid bilayer, what is the smaller number of amino acid helixes required for that helix to still span the lipid bilayer? c. How many hydrogen bonding interactions would there be in the smallest possible tilted transmembrane α-helix? d. If the tilted α-helix was a 310 helix instead how many amino acid residues would be required to span the lipid bilayer? How many amino acid residues would be required if it was a π-helix?arrow_forward
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