Campbell Biology in Focus
3rd Edition
ISBN: 9780134710679
Author: Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky, Rebecca Orr
Publisher: PEARSON
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Textbook Question
Chapter 3, Problem 6TYU
The structural level of a protein least a fleeted by a disruption in hydrogen bonding is the
- A. primary level.
- B. secondary level.
- C. tertiary level.
- D. quaternary level.
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Match the level of protein structure to its description:
Primary
Secondary
Tertiary
Quaternary
A.
Folding due to interactions among the peptide backbone
B.
Interactions among multiple polypeptide chains
C.
Sequence of amino acids
D.
Folding due to interactions among side chains
Protein Structure and Folding:a. Explain how changes in a protein’s amino acid sequence can change the way it behaves in water.b. Explain how changes in a protein’s amino acid sequence can change the way it interacts with othermolecules.c. Explain how changes in a protein’s amino acid sequence can change the way it forms secondary andtertiary structures when placed in water.
Which of the following statements is/are TRUE for globular proteins?
A. sensitive to changes in pH & heat
B. regular amino acid sequence
C. soluble in water
D. structural role
Chapter 3 Solutions
Campbell Biology in Focus
Ch. 3.1 - How are gasoline and fat chemically similar?Ch. 3.1 - Which molecules in Figure 3.4a re isomers? For...Ch. 3.1 - Prob. 3CCCh. 3.1 - Prob. 4CCCh. 3.2 - How many molecules of water are needed to...Ch. 3.2 - WHAT IF? Suppose you eat a serving of fish. What...Ch. 3.3 - Write the formula for a monosaccharide that has...Ch. 3.3 - A dehydration reaction joins two glucose molecules...Ch. 3.3 - WHAT IF? After a cow is given antibiotics to treat...Ch. 3.4 - Compare the structure of a fat (triglyceride) with...
Ch. 3.4 - Why are human sex hormones considered lipids?Ch. 3.4 - Prob. 3CCCh. 3.5 - Why does a denatured protein no longer function...Ch. 3.5 - What parts of a polypeptide participate in the...Ch. 3.5 - WHAT IF? Where would you expect a polypeptide...Ch. 3.6 - DRAW IT Go to Figure 3.27a and, for the top three...Ch. 3.6 - Prob. 2CCCh. 3.7 - How would sequencing the entire genome of an...Ch. 3.7 - Given the function of DNA, why would you expect...Ch. 3 - Which functional group is not present in this...Ch. 3 - MAKE CONNECTIONS Which chemical group is most...Ch. 3 - Prob. 3TYUCh. 3 - Which of the following statements concerning...Ch. 3 - Prob. 5TYUCh. 3 - The structural level of a protein least a fleeted...Ch. 3 - Enzymes that break down DNA catalyze the...Ch. 3 - Prob. 8TYUCh. 3 - The molecular formula for glucose is C6H12O6. What...Ch. 3 - Construct a table that organizes the following...Ch. 3 - Prob. 11TYUCh. 3 - Prob. 12TYUCh. 3 - FOCUS ON ORGANIZATION Proteins, which have diverse...Ch. 3 - Prob. 14TYUCh. 3 - SYNTHESIZE YOUR KNOWLEDGE Given that the function...
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- Which of the following statements about proteins is FALSE? a They can be hydrophobic, hydrophilic, or both. b They are composed of amino acids. c Their primary function is energy storage. d They have multiple levels of structural organization.arrow_forwardThe structural level of a protein least affected by a disruption in hydrogen bonding is the a. primary b.secondary c. tertiary d. quaternaryarrow_forwardBiological activity of proteins is dependent on which? A. peptide bonds B. thermodynamic properties C. an aqueous environment D. protein conformationarrow_forward
- Which level(s) of protein structure result(s) from non-covalent interactions involving both backbone groups and side chains? (Select all that apply!) a) Primary b) Secondary c) Tertiary d) Quaternaryarrow_forwardThe tertiary structure of a protein is established by: a. The sequence of amino acids in the protein b. The molecular weight of the protein c. The total number of amino acids in the protein d. The number of disulfide bridges in the protein e. The net charge of the the protein at physioloical pH.arrow_forwardThe difference between a polypeptide and a protein is a. that proteins are polypeptides folded up into a functional three-dimensional conformation b. that proteins are precursors of polypeptides c. that polypeptides are made of protein folded up into a functional three-dimensional conformation d. that proteins are always made with many polypeptidesarrow_forward
- This structure of a protein comes from the further bending and folding of pleated sheets and helices: A. primary B. secondary C. tertiary D. quaternaryarrow_forwardThe level of protein structure that describes all aspects of the three-dimensional folding of a polypeptide is referred to as the A. quaternary structure. B. secondary structure. C. primary structure. D. tertiary structure.arrow_forwardDenaturation of a protein A. adds hydrogen bonds to the primary level of protein structure. B. breaks hydrogen bonds in the primary level of protein structure. C. adds hydrogen bonds to the secondary and tertiary levels of protein structure. D. breaks hydrogen bonds in the secondary and tertiary levels of protein structure.arrow_forward
- Which of the following bonding types is the most important in the nonaqueous interfaces between protein subunits? a. van der Waals interactions b. the hydrophobic effect c. ionic bonds d. disulfide bridgesarrow_forwardWhich of the following statement about quaternary structure of protein is correct? Select one: a. Quaternary structure is a force between different polypeptides. b. Hydrogen bond is an only force found in quaternary structure. c. Quaternary structure contains one polypeptide. d. Quaternary structure is an unfolded form of protein.arrow_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_forward
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