α-Keratin is an intermediate filament with a basic structural unit of two a helices in a coiled coil. Each helix has a seven-residue repeating unit (heptad repeat). A representation of the a helices of a coiled coil dimer is shown. Each letter represents a different amino acid residue. f g d e Review the table of amino acids. a d g f Identify the three true statements about the structure of keratin. ☐ The a helix of the coiled coil is wound less tightly than predicted for an α helix. ☐ Each polypeptide in the dimer has 3.6 residues per turn, and a nonpolar group occurs every 3.5 residues, resulting in a slight winding, or twist, around the other polypeptide, forming a coiled coil. Arg-Ala-His-Glu-His-Thr-Asp is a likely repeat in the a helix of keratin. ☐ Val-Thr-Asp-Ala-Glu-Arg-His is a likely repeat in the a helix of keratin. ☐ The residues at positions b and c are less likely to be polar or charged because they are in contact with the solvent. ☐ Keratin molecules are very strong due to hydrophilic interactions between charged amino acid side chains.
α-Keratin is an intermediate filament with a basic structural unit of two a helices in a coiled coil. Each helix has a seven-residue repeating unit (heptad repeat). A representation of the a helices of a coiled coil dimer is shown. Each letter represents a different amino acid residue. f g d e Review the table of amino acids. a d g f Identify the three true statements about the structure of keratin. ☐ The a helix of the coiled coil is wound less tightly than predicted for an α helix. ☐ Each polypeptide in the dimer has 3.6 residues per turn, and a nonpolar group occurs every 3.5 residues, resulting in a slight winding, or twist, around the other polypeptide, forming a coiled coil. Arg-Ala-His-Glu-His-Thr-Asp is a likely repeat in the a helix of keratin. ☐ Val-Thr-Asp-Ala-Glu-Arg-His is a likely repeat in the a helix of keratin. ☐ The residues at positions b and c are less likely to be polar or charged because they are in contact with the solvent. ☐ Keratin molecules are very strong due to hydrophilic interactions between charged amino acid side chains.
Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
Section: Chapter Questions
Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...
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Transcribed Image Text:α-Keratin is an intermediate filament with a basic structural unit of two a helices in a coiled coil. Each helix has a seven-residue
repeating unit (heptad repeat). A representation of the a helices of a coiled coil dimer is shown. Each letter represents a different
amino acid residue.
f
g
d
e
Review the table of amino acids.
a
d
g
f
Identify the three true statements about the structure of keratin.
☐ The a helix of the coiled coil is wound less tightly than predicted for an α helix.
☐ Each polypeptide in the dimer has 3.6 residues per turn, and a nonpolar group occurs every 3.5 residues, resulting in a
slight winding, or twist, around the other polypeptide, forming a coiled coil.
Arg-Ala-His-Glu-His-Thr-Asp is a likely repeat in the a helix of keratin.
☐ Val-Thr-Asp-Ala-Glu-Arg-His is a likely repeat in the a helix of keratin.
☐ The residues at positions b and c are less likely to be polar or charged because they are in contact with the solvent.
☐ Keratin molecules are very strong due to hydrophilic interactions between charged amino acid side chains.
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