Biological Science
5th Edition
ISBN: 9780321743671
Author: Scott Freeman
Publisher: PEARSON
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Chapter 3, Problem 4TYK
Summary Introduction
Introduction:
Amino acids essentially are considered to be the building blocks of life as they are the basic units of a protein that carry out functions in the body. The structure of an amino acid residue includes a carbon atom to which a carboxylic group, a hydrogen atom, an amino group, and an alkyl group are attached. There are a total of 22 amino acids that occur in nature.
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Students have asked these similar questions
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.
A polypeptide with a net positive charge at physiologic pH (~7.4) most likely contains amino acids with R groups of what type?
a. Acidic R groups
b. Aromatic R groups
c. Aliphatic R groups
d. Basic R groups
Using a diagram, show why a peptide bond is planar. Why are cis peptide bonds uncommon or rate in proteins?
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- Choose one for each question given: A. quaternary level B. tertiary level C. primary level D. secondary levelarrow_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_forwardDraw out the structural formula of the oligopeptide, with the first amino acid as the N-terminusarrow_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_forwardWhich is a difference between an alpha-helix and a beta-pleated sheet? Select one: a. An alpha-helix contains mainly amino acids with polar R-groups while a beta- pleated sheet contains mainly amino acids with non-polar R-groups. b. An alpha-helix contains disulfide bonds while a beta-pleated sheet contains ionic bonds. c. An alpha-helix has non-covalent bonds between amino acids near each other in the sequence while a beta-pleated sheet has non-covalent bonds between amino acids far apart in the sequence. d. An alpha-helix has a spiral shape while a beta-pleated sheet has a compact zig-zag shape.arrow_forwardWhat 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_forward
- Draw and label the dinucleotide AT as follows: A. 5’ and 3’ ends B. Phosphodiester bond C. N-glycosidic bondsarrow_forwardWhat 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_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
- What is the length of an α-helical section of a polypeptide chain of 20 residues? How do you calculate this? 90 Å 60 Å 30Å 9 Å 3 Åarrow_forwardOn the image below, label the structures below (image is in color-view it online). "Not present" is an acceptable answer. a. Alpha helix b. Beta sheet C. Hydrophobic core d. Random coil е. Reasonable location for a proline f. Draw in the appropriate hydrogen bonds for stabilizing the secondary structure for one alpha helix and one beta sheet. If the structure is not present, write that here.arrow_forwardAssume you want to make and study fragments of a protein. Would you expect that any fragment of the polypeptide chain would fold the same way as it would in the intact protein?arrow_forward
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