Campbell Biology In Focus, Loose-leaf Edition (3rd Edition)
3rd Edition
ISBN: 9780134895727
Author: Lisa A. Urry, Michael L. Cain, Steven A. Wasserman, Peter V. Minorsky
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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The 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.
Denaturation 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.
Which 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.
Chapter 3 Solutions
Campbell Biology In Focus, Loose-leaf Edition (3rd Edition)
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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- The 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_forwardMatch 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 chainsarrow_forwardThe structure of a protein results from the folding ofthe pleated sheets or helices.a. primary c. tertiaryb. secondary d. quaternaryarrow_forward
- Variations in three-dimensional shapes among proteins are due tobonding between thea. amino groups.b. R groups.c. ion groups.d. H atomsarrow_forwardThis 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 structural level of a protein least affected by a disruption in hydrogen bonding is the a. primary b.secondary c. tertiary d. quaternaryarrow_forward
- Large globular proteins frequently are comprised of two or more recognizable structures that often confer unique functions or properties. These structures are termed: a quatemary structure b. domains c. heterotropic d. multimeric e à andearrow_forwardAt what level(s) of protein structure would you expect to find disulfide bridges? a. primary O b. secondary O c. tertiary d. quaternary e. only in b and carrow_forwardWhich of the following is NOT an example of protein secondary structure? a. alpha-helix b. beta sheets c. beta turn d. coiled coil e. loopsarrow_forward
- A. A macromolecule composed of one or more polypeptides B. The monomer of polypeptides. C. The specific sequence of amino acids in a polypeptide. D. Structure of coils and/or folds of a polypeptide strueture. E. Structure of polypeptide resulting from interactions between R-groups. Contributes to unique 3D shape of molecule. F. Two or more polypeptides interacting to form a single functional unit. 1. Protein 2. amino acid 3. primary structure 4. secondary structure 5. tertiary structure 6. quaternary structurearrow_forwardWhich 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 statements are correct about protein structure (select all that apply)? A. Post-translational modifications such as glycosylation or phosphorylation may alter the structure of a protein B. Only amino acids with a net charge may interact with other amino acids C. The 3D structure of a protein is determined primarily by the protein backbone/main chain conformation while the amino acid sidechains play only a minor role. D. Hydrophobic interactions play a key role in protein folding E. Amino acid sidechains contribute to 3D structure through their ability to form hydrogen bonds with other amino acidsarrow_forward
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