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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Students have asked these similar questions
The unique cyclic structure of which of the
following amino acids plays a central role in the
formation of alpha helices and beta sheets?
Please choose from one of the following options.
Select one:
a. Lysine
b. Arginine
c. Proline
d. Valine
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.
Beta-sheets are roughly planar structures, in which the backbone hydrogen bonding pattern defines the plane.
Where are the side chains in a sheet?
Select one:
a. The side-chains are on the outside of the sheet.
O b. The side-chains are in the plane of the sheet, with residues from one chain on one side of the sheet, and
residues from the other chain being on the other side.
The side-chains do not have a consistent pattern.
d. The side-chains are perpendicular to the plane of the sheet, with residues from one chain being above and
residues from the other being below the plane of the sheet.
C.
e.
The side-chains are perpendicular to the plane of the sheet, with residues from each chain alternating
between above and below the plane of the sheet.
O f.
The side-chains are in the plane of the sheet, with residues from each chain alternating being on one side or
the other of the sheet.
g. Beta-sheets are rarely observed in proteins.
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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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.Similar questions
- What is the general characteristic of protein domains? A. All protein domains exhibit both a and B structures B. Protein domains constitute supersecondary structures that have specific biological functions in proteins. C. Most protein domains can be hydrolyzed from parent polypeptide chains while retaining functions and/or structures that are conserved. D. Protein domains constitute the structural block from which the protein is built E. Protein domains contain motifs that are the binding sites for prosthetic groups such as heme, or the iron-sulfur clusters.arrow_forwardConsider the hydrogen bonding pattern of an α-helix with the following sequence: HLRTNAGCSY Asparagine’s amide hydrogen is hydrogen bonded to: a. Serine’s side chain b. Histidine’s backbone carbonyl oxygen c. Cysteine’s backbone carbonyl oxygen d. Serine’s backbone carbonyl oxygen e. Histidine’s side chainarrow_forwardSelect the amino acids that are most likely to participate in hydrophobic interations. SELECT ALL THAT APPLY A. Valine B. Leuicine C. Phenylalanine D. Aspartatearrow_forward
- Which statement is true regarding an a helix, there are five residues per helical turn. the helix is right-handed there are usually many proline residues present. side chain residues point up and down the axis of the helix.arrow_forwardWhich of the following statement about proteins is correct a. alpha helix and Beta pleated sheets are considered quaternary structures b. a single polypeptide only has primary sytructure, secondary, tertiary, and quaternary structures require more than one polypeptide c. there are 30 essential amino acids that are the monomer building blocks of proteins d. polypeptides have a distinct polarity (directionality) with one end refered to as the free amino end, and the other called the free carboxyl endarrow_forwardWhat is the hydrogen bonding pattern within an alpha helix? a. Lone pair on C=O of residue i to hydrogen on N-H of residue i+3. b. Lone pair on C=O of residue i to hydrogen on N-H of residue i+4. c. Hydrogen of N-H of residue i to hydrogen on N-H of residue i+3. d. Lone pair on C=O of residue i to hydrogen on N-H of residue i+2.arrow_forward
- Imagine the main chain of a protein bends back on itself, so that two amino acid residues R, and R, come close to each other. In the table below are four possibilities for what R, and R, might be. In each case, decide whether a specific interaction could form between the residues. If a specific interaction could form, give the name of the interaction. R₁ R₂ threonine cysteine glutamine arginine cysteine tyrosine phenylalanine glutamate specific interaction? Oyes no yes O no O yes O no Oyes O no name of specific interaction 0 0 0 0 Xarrow_forwardA 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_forwardWhich amino acids are most likely found in the transmembrane portion of an alpha helix? a. Lysine b. Phenylalanine c. Aspartate d. Glutamate e. All of themarrow_forward
- Choose one for each question given: A. quaternary level B. tertiary level C. primary level D. secondary levelarrow_forwardProline is sometimes found as one of the first four residues of an alpha helix. Proline is less frequently found in the center of a helix, but is also relatively often observed as the first non-helical residue after the end of a helix. Why is this true? Select one: a. Proline cannot hydrogen bond, and therefore it does not participate in secondary structure. O b. Proline is too flexible to fit properly into a helix, and therefore is rarely found in helix structures for entropic reasons. c. When part of a polypeptide, proline lacks the amide proton. Therefore, in a helix, it does not hydrogen bond to residues earlier in the helix. However, the first four residues of a helix by definition cannot hydrogen bond to earlier residues in the helix, so this does not matter. d. Proline cannot adopt the phi and psi angles necessary to fit properly into a helix. e. Proline is a rare amino acid and therefore it rarely is found anywhere.arrow_forwardHow can you describe the hydrogen bonding pattern of alpha helices? a. NH of residue n with CO of residue n+3 b. CO of residue n with NH of residue n+3 c. NH of residue n with CO of residue n+4 d. CO of residue n with NH of residue n+4arrow_forward
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