Exam 3: Protein Structure and Function
Exam 1: Biology and the Tree of Life40 Questions
Exam 2: Water and Carbon: the Chemical Basis of Life50 Questions
Exam 3: Protein Structure and Function47 Questions
Exam 4: Nucleic Acids and the Rna World33 Questions
Exam 5: An Introduction to Carbohydrates30 Questions
Exam 6: Lipids, membranes, and the First Cells47 Questions
Exam 7: Inside the Cell28 Questions
Exam 8: Cell-Cell Interactions27 Questions
Exam 9: Cellular Respiration and Fermentation27 Questions
Exam 10: Photosynthesis32 Questions
Exam 11: The Cell Cycle31 Questions
Exam 12: Meiosis34 Questions
Exam 13: Mendel and the Gene32 Questions
Exam 14: Dna and the Gene: Synthesis and Repair37 Questions
Exam 15: How Genes Work34 Questions
Exam 16: Transcription and Translation38 Questions
Exam 17: Control of Gene Expression in Bacteria31 Questions
Exam 18: Control of Gene Expression in Eukaryotes37 Questions
Exam 19: Analyzing and Engineering Genes40 Questions
Exam 20: Genomics38 Questions
Exam 21: Principles of Development25 Questions
Exam 22: An Introduction to Animal Development22 Questions
Exam 23: An Introduction to Plant Development21 Questions
Exam 24: Evolution by Natural Selection32 Questions
Exam 25: Evolutionary Processes32 Questions
Exam 26: Speciation33 Questions
Exam 27: Phylogenies and the History of Life38 Questions
Exam 28: Bacteria and Archaea38 Questions
Exam 29: Protists34 Questions
Exam 30: Green Plants49 Questions
Exam 31: Fungi37 Questions
Exam 32: An Introduction to Animals38 Questions
Exam 33: Protostome Animals38 Questions
Exam 34: Deuterostome Animals46 Questions
Exam 35: Viruses31 Questions
Exam 36: Plant Form and Function39 Questions
Exam 37: Water and Sugar Transport in Plants42 Questions
Exam 38: Plant Nutrition36 Questions
Exam 39: Plant Sensory Systems, signals, and Responses66 Questions
Exam 40: Plant Reproduction41 Questions
Exam 41: Animal Form and Function29 Questions
Exam 42: Water and Electrolyte Balance in Animals38 Questions
Exam 43: Animal Nutrition37 Questions
Exam 44: Gas Exchange and Circulation37 Questions
Exam 45: Electrical Signals in Animals33 Questions
Exam 46: Animal Sensory Systems and Movement36 Questions
Exam 47: Chemical Signals in Animals33 Questions
Exam 48: Animal Reproduction34 Questions
Exam 49: The Immune System in Animals32 Questions
Exam 50: An Introduction to Ecology38 Questions
Exam 51: Behavioral Ecology37 Questions
Exam 52: Population Ecology46 Questions
Exam 53: Community Ecology39 Questions
Exam 54: Ecosystems41 Questions
Exam 55: Biodiversity and Conservation Biology39 Questions
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The lock-and-key analogy for enzymes applies to the _____.
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(Multiple Choice)
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Correct Answer:
C
At the pH found in cells (about 7.0),what happens to the amino group on an amino acid?
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Correct Answer:
A
Suppose you discovered a new amino acid.Its R-group contains only hydrogen and carbon atoms.Predict the behavior of this amino acid.
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Correct Answer:
A
Aquaporins are proteins that control the passage of water molecules across the cell membrane.The protein forms a pore,or opening,in the membrane.You isolate what you think are two different molecules of aquaporin,and determine that one of the proteins has a larger pore diameter than the second.Which of the following do you conclude?
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In cells,the activity of enzymes is often regulated by other molecules.Why is this necessary?
(Multiple Choice)
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You collect data on the effect of pH on the function of the enzyme catalase in human cells.Which of the following graphs would you expect?
(Multiple Choice)
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What type of interaction is directly responsible for the formation of secondary structure?
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Refer to the following paragraph and Figure 3.1 to answer the following questions.
Figure 3.1
Since structure correlates so well with function,biochemists are constantly looking for new ways to probe the complex structure of proteins in order to understand what they do and how they do it.One of the most powerful techniques in existence today is X-ray crystallography.The main difficulty with this technique is getting the protein to crystallize.Once crystallized,the protein is bombarded with X-rays to create a pattern that can be analyzed mathematically to determine the three-dimensional structure of the protein.This analysis has been performed by Krzysztof Palczewski on the protein rhodopsin,which is a light-sensitive protein found in species ranging from ancient bacteria (archaea)to humans.The structure (schematically shown above,where each letter represents an amino acid)is characterized by a single polypeptide chain with several α-helical segments that loop back and forth across the cell membrane.Another notable feature is the disulfide bond (-S-S-)that can be seen at the bottom of the third transmembrane segment.[Figure adapted from K.Palczewski et al. ,Science 289 (2000): 739.]
-How many times does the protein in Figure 3.1 cross the cell membrane?
![Refer to the following paragraph and Figure 3.1 to answer the following questions. Figure 3.1 Since structure correlates so well with function,biochemists are constantly looking for new ways to probe the complex structure of proteins in order to understand what they do and how they do it.One of the most powerful techniques in existence today is X-ray crystallography.The main difficulty with this technique is getting the protein to crystallize.Once crystallized,the protein is bombarded with X-rays to create a pattern that can be analyzed mathematically to determine the three-dimensional structure of the protein.This analysis has been performed by Krzysztof Palczewski on the protein rhodopsin,which is a light-sensitive protein found in species ranging from ancient bacteria (archaea)to humans.The structure (schematically shown above,where each letter represents an amino acid)is characterized by a single polypeptide chain with several α-helical segments that loop back and forth across the cell membrane.Another notable feature is the disulfide bond (-S-S-)that can be seen at the bottom of the third transmembrane segment.[Figure adapted from K.Palczewski et al. ,Science 289 (2000): 739.] -How many times does the protein in Figure 3.1 cross the cell membrane?](https://storage.examlex.com/TB3734/11ea48b8_22eb_9c66_b057_b92d39768e23_TB3734_00_TB3734_00_TB3734_00_TB3734_00_TB3734_00_TB3734_00.jpg)
(Multiple Choice)
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What is the pattern component of the theory of chemical evolution?
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An enzyme has a total of four active sites.When you denature the molecule and study its composition,you find that each active site occurs on a different polypeptide.Which of the following hypotheses does this observation support?
(Multiple Choice)
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At the pH found in cells (about 7.0),what happens to the carboxyl group on an amino acid?
(Multiple Choice)
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Refer to the following paragraph and Figure 3.1 to answer the following questions.
Figure 3.1
Since structure correlates so well with function,biochemists are constantly looking for new ways to probe the complex structure of proteins in order to understand what they do and how they do it.One of the most powerful techniques in existence today is X-ray crystallography.The main difficulty with this technique is getting the protein to crystallize.Once crystallized,the protein is bombarded with X-rays to create a pattern that can be analyzed mathematically to determine the three-dimensional structure of the protein.This analysis has been performed by Krzysztof Palczewski on the protein rhodopsin,which is a light-sensitive protein found in species ranging from ancient bacteria (archaea)to humans.The structure (schematically shown above,where each letter represents an amino acid)is characterized by a single polypeptide chain with several α-helical segments that loop back and forth across the cell membrane.Another notable feature is the disulfide bond (-S-S-)that can be seen at the bottom of the third transmembrane segment.[Figure adapted from K.Palczewski et al. ,Science 289 (2000): 739.]
-What is the location of the C-terminus of the protein in Figure 3.1?
![Refer to the following paragraph and Figure 3.1 to answer the following questions. Figure 3.1 Since structure correlates so well with function,biochemists are constantly looking for new ways to probe the complex structure of proteins in order to understand what they do and how they do it.One of the most powerful techniques in existence today is X-ray crystallography.The main difficulty with this technique is getting the protein to crystallize.Once crystallized,the protein is bombarded with X-rays to create a pattern that can be analyzed mathematically to determine the three-dimensional structure of the protein.This analysis has been performed by Krzysztof Palczewski on the protein rhodopsin,which is a light-sensitive protein found in species ranging from ancient bacteria (archaea)to humans.The structure (schematically shown above,where each letter represents an amino acid)is characterized by a single polypeptide chain with several α-helical segments that loop back and forth across the cell membrane.Another notable feature is the disulfide bond (-S-S-)that can be seen at the bottom of the third transmembrane segment.[Figure adapted from K.Palczewski et al. ,Science 289 (2000): 739.] -What is the location of the C-terminus of the protein in Figure 3.1?](https://storage.examlex.com/TB3734/11ea48b8_22eb_9c66_b057_b92d39768e23_TB3734_00_TB3734_00_TB3734_00_TB3734_00_TB3734_00_TB3734_00.jpg)
(Multiple Choice)
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Which one of the following is not a component of each monomer used to make proteins?
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A series of hydrophobic side chains will congregate together as a protein folds in an aqueous solution and be stabilized by _____.
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HIV is the virus that causes AIDS.In the mid-1990s,researchers discovered an enzyme in HIV called protease.Once the enzyme's structure was known,researchers began looking for drugs that would fit into the active site and block it.If this strategy for stopping HIV infections were successful,it would be an example of what phenomenon?
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You've just sequenced a new protein found in mice and observe that sulfur-containing cysteine residues occur at regular intervals.What is the significance of this finding?
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Which of the following observations is the strongest argument in favor of the hypothesis that protein structure and function are correlated?
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You disrupt all hydrogen bonds in a protein.What level of structure will be preserved?
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