Exam 6: Proteins: Three-Dimensional Structure
Exam 1: Introduction to the Chemistry of Life56 Questions
Exam 2: Water59 Questions
Exam 3: Nucleotides, nucleic Acids, and Genetic Information67 Questions
Exam 4: Amino Acids68 Questions
Exam 5: Proteins: Primary Structure68 Questions
Exam 6: Proteins: Three-Dimensional Structure60 Questions
Exam 7: Protein Function Part I: Myoglobin and Hemoglobin74 Questions
Exam 8: Carbohydrates66 Questions
Exam 9: Lipids and Biological Membranes58 Questions
Exam 10: Membrane Transport49 Questions
Exam 11: Enzyme Catalysis53 Questions
Exam 12: Enzyme Kinetics, inhibition and Control54 Questions
Exam 13: Biochemical Signaling50 Questions
Exam 14: Introduction to Metabolism52 Questions
Exam 15: Glucose Catabolism50 Questions
Exam 16: Glycogen Metabolism and Gluconeogenesis50 Questions
Exam 17: Citric Acid Cycle50 Questions
Exam 18: Electron Transport and Oxidative Phosphorylation50 Questions
Exam 19: Photosynthesis50 Questions
Exam 20: Lipid Metabolism51 Questions
Exam 21: Amino Acid Metabolism50 Questions
Exam 22: Mammalian Fuel Metabolism: Integration and Regulation50 Questions
Exam 23: Nucleotide Metabolism50 Questions
Exam 24: Nucleic Acid Structure50 Questions
Exam 25: DNA Replication, repair and Recombination50 Questions
Exam 26: Transcription and Rna Processing50 Questions
Exam 27: Protein Synthesis49 Questions
Exam 28: Regulation of Gene Expression50 Questions
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-________ is a fibrous protein that contains a hydrophobic amino acid approximately every 4 residues which forms an α helix with one hydrophobic side.
Free
(Multiple Choice)
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Correct Answer:
B
Matching
-Repeating values of and make up predictable orientations of amino acid with a chain,this predictable orientation forms___________.
Free
(Multiple Choice)
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Correct Answer:
H
The low pH found in the gut can enhance the digestibility of dietary protein by causing ___.
Free
(Multiple Choice)
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Correct Answer:
B
Noncovalent forces that stabilize protein structure include all of the following except __________.
(Multiple Choice)
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Which of the following would be most stable based on the information you have learned about protein structure?
(Multiple Choice)
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Which of the following gives the best example of a nonrepetitive structure in a protein?
(Multiple Choice)
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Which of the following structural proteins has the greatest elasticity?
(Multiple Choice)
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The first step in the folding of disordered polypeptides into ordered functional protein is the formation of ______.
(Multiple Choice)
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Which of the following has (have)both a favorable hydrogen bonding pattern and and values that fall within the allowed Ramachandran conformational regions?
(Multiple Choice)
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Of the following,which amino acid is most likely to be found in position 1 or 4 on α keratin?
(Multiple Choice)
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Which of the following is true regarding crystalline proteins?
(Multiple Choice)
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Examine the three sequences below for collagen-like proteins.If hydrogen bonding were the most important feature in determining strength in fibrous proteins,which of the following sequences likely has the highest melting temperature and why? (Note: Flp = fluoroproline;Hyp = hydroxyproline)
(I)Pro-Hyp-Gly-Pro-Hyp-Gly-Pro-Hyp-Gly
(II)Pro-Flp-Gly-Pro-Flp-Gly-Pro-Flp-Gly
(III)Gly-Pro-Thr-Gly-Pro-Thr-Gly-Pro-Thr
(Multiple Choice)
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Conventional one dimensional NMR spectroscopy is not generally an effective tool for determination of protein structure because…
(I)Proteins (including small proteins)have a high number of hydrogen atoms.
(II)NMR requires a high quality protein crystal.
(III)The NMR spectra exhibit high peak overlap.
(Multiple Choice)
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-The strength of _______ comes from close packing of glycine residues and the characteristics of hydroxyproline allowing formation of a left- handed helical conformation which combines with two other left handed structures to form a right-handed triplet helix.
(Multiple Choice)
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-In a ______,the and angles of the peptide backbone would orient atoms closer than their van der Waals distance.
(Multiple Choice)
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The Protein Data Bank (PDB)is a database provides structural information about proteins that may be useful for which of the following?
(I)A researcher studying the changes in protein fold associated with prions.
(II)A researcher classifying structural elements by function.
(III) A researcher designing a compound to bind tightly to a particular region in the protein.
(Multiple Choice)
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Which of the following changes would not alter the functional characteristics of α keratin?
(Multiple Choice)
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In a protein,the most conformationally restricted amino acid is ______;the least conformationally restricted is ______.
(Multiple Choice)
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What observation about protein refolding or renaturation helped to solidify the connection between primary amino acid sequence and 3-D structure?
(Multiple Choice)
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