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Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN: 9780134580999
Author: Elaine N. Marieb, Katja N. Hoehn
Publisher: PEARSON
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
Transcribed Image Text:Which of the following features correctly describe aspects of protein structure?
a) A protein possessing disulfide bonds will be more stable than a protein with the
identical primary sequence lacking disulfide bonds.
O b) B-sheets can only be formed from the anti-parallel arrangement of B-strands.
c) Folding of a protein (tertiary structure) will typically result in a majority of the
non-polar amino acids being distributed on the protein surface.
d) both a and c

Transcribed Image Text:Asymmetrical distribution of membrane phospholipids in cytosolic versus extracellular
leaflets of the plasma membrane is largely due to...
the tendency of hydrophobic phospholipids to avoid the extracellular fluid by
flipping to the inner membrane leaflet.
scramblase enzymes in the ER that catalyze the movement of phosphatidyl
b)
serine and phosphatidyl ethanolamine (PS, PE) from cytosolic to non-cytosolic
membrane leaflets.
scramblase enzymes in the plasma membrane that catalyze the movement of
phosphatidyl serine and phosphatidyl ethanolamine (PS, PE) from outer to inner
membrane leaflets.
flippase enzymes in the Golgi apparatus that catalyze the movement of
d)
phosphatidyl serine and phosphatidyl ethanolamine (PS, PE) from one
membrane leaflet to the other.
e) both b and d are true.
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- 1. What is the isoelectric point (pI) of lysine which has pKa values of 2.1 for the α carboxyl group, 9.7 for the α amino group and 10.5 for the side chain amino group? 2. Which of the following is most likely to be found on the exterior of a protein? A) Pro B) Trp C) Ser D) Glu 3. The type of reaction that forms a peptide bond is A) Elimination B) Hydrolysis C) Nucleophilic substitution D) Condensationarrow_forwardWhich of the following levels of protein structure can involve covalent bond formation? A) Primary B) Secondary C) Teritary D) Quaternary E) Primary and teritary F) Primary, teritary and quaternaryarrow_forwarda helix and B pleated sheets are what protein structure? primary, tertiary, secondary, or quaternary?arrow_forward
- Which of the following, if any, is correct about protein folding? a)2° structure formation is primarily entropic, 3° structure formation is primarily entropic b)2° structure formation is primarily entropic, 3° structure formation is primarily enthalpic c)2° structure formation is primarily enthalpic, 3° structure formation is primarily entropic d)2° structure formation is primarily enthalpic, 3° structure formation is primarily enthalpic e)None of the abovearrow_forwardDescribe the 4 levels of protein structure: primary, secondary, tertiary and quaternary. And, note which will be disrupted by application of heat.arrow_forwardProtein structures have several different levels of organization. In the space below indicate the type of molecular bonds that can contribute to each level of organization: primary- secondary- tertiary- quarternary-arrow_forward
- The tertiary structure of a protein is the 3-dimensional folding of the polypeptide chain. What types of bonds support the folding of proteins into this level of protein structure? Also, how do these bonds/interactions impact how a protein folds and its surface properties? Can the tertiary structure of a protein depend on the type of cell system used for synthesis? Explain.arrow_forwardWhich of the following is an example of secondary protein structure?A) DipeptideB) TriglycerideC)α -helixD) Amino acidE) Fatty acidarrow_forwardA) Briefly describe the basic structure of phospholipids and explain how they can provide an effective barrier against the unregulated movement of molecules into or out of cells. B) Not all phospholipids are identical to one another. Describe two components (parts) of that can be altered to create variation between different phospholipids.arrow_forward
- 3. Which best describes the contribution of tertiary (3’) structure of to the native conformation of polypeptides and proteins: a) Structure that results from intrachain interactions of amino acid side chains b) Structure that results from interchain interactions of amino acid side chains c) Structure that results from base pairing d) Structure that results from the linear sequence of amino acids from beginning to end of moleculearrow_forwardThe following diagram shows a short piece of a protein. Use the diagram to answer the following questions. A. What three amino acids are present in the segment? B. How many peptide bonds are present? C. Which amino acid is at the N terminus?arrow_forwardA mutation leads to a change in amino acid from valine, an amino acid with a nonpolar side chain, to aspartic acid, an amino acid with a polar, negatively-charged side chain. Do you think that the following levels of protein structure change? If so, how and why? If not, why not? Please frame your answer in terms of chemical bonds and interactions. (primary structure, secondary structure, tertiary structure, quartenary structure)arrow_forward
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