EP CAMPBELL BIO.IN FOCUS AP-MOD.MASTER.
3rd Edition
ISBN: 9780137453092
Author: Urry
Publisher: SAVVAS L
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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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Students have asked these similar questions
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.
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
Chapter 3 Solutions
EP CAMPBELL BIO.IN FOCUS AP-MOD.MASTER.
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 structure of a protein results from the folding ofthe pleated sheets or helices.a. primary c. tertiaryb. secondary d. quaternaryarrow_forwardVariations 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_forward
- The structural level of a protein least affected by a disruption in hydrogen bonding is the a. primary b.secondary c. tertiary d. quaternaryarrow_forwardLarge 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_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 the native state of a protein (select all that apply)? A. Polar sidechains commonly interact with water B. Hydrophobic amino acids tend to be on surface of protein C. The sidechains of polar amino acids are most commonly found in the central core of a protein D. Formation of an alpha-helix is primarily driven by hydrogen bonds between the protein main chain, not sidechains. E. Secondary structure is largely driven by hydrophobic interactionsarrow_forward
- Which 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_forwardThe bonds that are important inthe secondary structure of a protein are a)hydrogen bonds b.peptide bonds c.hydrophobic interaction d.salt bridges e.disulfide bondsarrow_forwardBoth alpha-helices and beta-sheets (select any/all answers that apply): A. are examples of secondary structure. B. are stabilized by hydrogen-bonds between backbone atoms. C. are examples of tertiary structures. D. never contain proline residues. E. are commonly found in proteins.arrow_forward
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