Human Anatomy & Physiology (11th Edition)
Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN: 9780134580999
Author: Elaine N. Marieb, Katja N. Hoehn
Publisher: PEARSON
Bartleby Related Questions Icon

Related questions

Question
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.
expand button
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.
Expert Solution
Check Mark
Knowledge Booster
Background pattern image
Similar questions
Recommended textbooks for you
Text book image
Human Anatomy & Physiology (11th Edition)
Biology
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:PEARSON
Text book image
Biology 2e
Biology
ISBN:9781947172517
Author:Matthew Douglas, Jung Choi, Mary Ann Clark
Publisher:OpenStax
Text book image
Anatomy & Physiology
Biology
ISBN:9781259398629
Author:McKinley, Michael P., O'loughlin, Valerie Dean, Bidle, Theresa Stouter
Publisher:Mcgraw Hill Education,
Text book image
Molecular Biology of the Cell (Sixth Edition)
Biology
ISBN:9780815344322
Author:Bruce Alberts, Alexander D. Johnson, Julian Lewis, David Morgan, Martin Raff, Keith Roberts, Peter Walter
Publisher:W. W. Norton & Company
Text book image
Laboratory Manual For Human Anatomy & Physiology
Biology
ISBN:9781260159363
Author:Martin, Terry R., Prentice-craver, Cynthia
Publisher:McGraw-Hill Publishing Co.
Text book image
Inquiry Into Life (16th Edition)
Biology
ISBN:9781260231700
Author:Sylvia S. Mader, Michael Windelspecht
Publisher:McGraw Hill Education