Biological Science (6th Edition)
6th Edition
ISBN: 9780321976499
Author: Scott Freeman, Kim Quillin, Lizabeth Allison, Michael Black, Emily Taylor, Greg Podgorski, Jeff Carmichael
Publisher: PEARSON
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Textbook Question
Chapter 3, Problem 2TYK
What type of bond is directly involved in the formation of an α-helix?
a. peptide bonds between amino acid residues
b. hydrogen bonds between amino acid residues
c. van der Waals interactions between nonpolar residues
d. disulfide bonds that form between cysteine residues
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a.Describe the bonds which hold a quaternary protein molecule together.
b. Discuss the reasons why glycine and proline are not usually found in an alpha helix of proteins.
How would adding acid to a non-buffered solution be most likely to affect protein structure?
Select one:
a. Adding acid would disrupt the primary structure of the protein
b. Adding acid would cause the protein to become a lipid
c. Adding acid would cause the protein to become a carbohydrate
d. Adding acid would disrupt the secondary and tertiary structure of the protein
A portion of a polypeptide chain contains the following sequence of amino acids: (-Met, -Leu, -Ala, -Cys, -Asp-) a.) Which amino acid can form a disulfide bond? b.) Which amino acids are likely to make the polypeptide more soluble in water? c.) Which amino acids are likely to make the polypeptide less soluble in water? d.) How does the primary structure of a protein affect its tertiary structure?
Chapter 3 Solutions
Biological Science (6th Edition)
Ch. 3 - 1. What two functional groups are bound to the...Ch. 3 - 2. What type of bond is directly involved in the...Ch. 3 - What type of information is used to direct...Ch. 3 - 4. What is an active site?
a. the location in an...Ch. 3 - Prob. 5TYUCh. 3 - Prob. 6TYUCh. 3 - 7. Why are proteins not considered to be a good...Ch. 3 - Prob. 8TYUCh. 3 - Prob. 9TYPSSCh. 3 - 10. Make a concept map (see BioSkills 12) that...
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- How do you answer this question: Describe the 'peptide backbone' of a polypeptide. How are the 'R' groups oriented along the peptide backbone of a polypeptide?arrow_forwardHow does a highly acidic solution denature proteins? A. The excess protons interfere with a protein’s ability to form peptide bonds. B. The lack of protons interferes with a protein’s ability to form peptide bonds. C. The lack of protons interferes with a protein’s ability to form secondary structures. D. The excess protons interfere with a protein’s ability to form secondary structures.arrow_forwardUse a rough diagram to compare the structures of a proteina-helix and an antiparallel b-sheet. For simplicity, showonly the backbone atoms of the protein.arrow_forward
- A short peptide of about 15 amino acids contains 3 Leu, 6 Val, and 3 Thr. What secondary structure is it most likely to adopt? Please answer with detailed reasonings. a. beta-sheet b. random unstructured coil c. hairpin turn (reverse turn) d. helix.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_forwardWhich of the following describes the tertiary structure of proteins? A. Helices and sheets formed from hydrogen bonds between the amino acids of polypeptides B. The functional domains that form from interactions between different parts of the polypeptide C. The association of multiple polypeptides D. The linear sequence of amino acids making up the polypeptidearrow_forward
- What is the primary reason the a-helix conformation in polypeptides such a stable form? A. The a-helix structure is stabilized by hydrophobic interactions. B. The a-helix structure is stabilized by intra-helical hydrogen bonds. C. The a-helix structure is stabilized by disulfide bonds. D. The a-helix structure is stabilized by proline residues.arrow_forwardWhat is the chemical difference between cellulose and chitin? Select one: a. Replacement of the hydroxyl group at C5 with an acetylated amino group b. Replacement of the hydroxyl group at C3 with an acetylated amino group c. Replacement of the hydroxyl group at C4 with an acetylated amino group d. Replacement of the hydroxyl group at C2 with an acetylated amino grouparrow_forwardShown below is an internal fragment of a polypeptide. If this polypeptide were growing, onto which end would the next amino acid be added? a) onto the right b) onto the leftarrow_forward
- Valine is an amino acid with a nonpolar side chain and serine is one with a polar side chain. Draw the two amino acids.(a) Why is the side chain for valine nonpolar, whereas the side chain for serineis polar?(b) Which amino acid has a hydrophilic side chain and which has a hydrophobic sidechain?arrow_forwardDraw a region of a polypeptide chain showing a hydrophobic pocket containing nonpolar side chains.arrow_forwardThe following diagram shows a short piece of a protein. Use the diagram to answer the following questions. A. What three amino acids are present in the segment? B. How many peptide bonds are present? C. Which amino acid is at the N terminus?arrow_forward
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