a-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. е g b С d a f f d a С е Identify the three true statements about the structure of keratin Ile-Lys-Asn-Leu-Asn- Glu-Thr is a likely repeat in the a helix of keratin. Glu-Leu-Thr-Asn-Thr-Lys-Cys is a likely repeat in the a helix of keratin. Keratin molecules are very strong due to hydrophilic interactions between charged amino acid side chains. The residues at positions b and c are less likely to be polar or charged because they are in contact with the solvent. The a helix of the coiled coil is wound less tightly than predicted for an a helix oa-Keratin is rich in Cys residues, enabling the formation of covalent cross-links between peptide chains and increasing the strength of the protein. Each polypeptide in the dimer has 3.6 residuess per turn, and a nonpolar group occurs every 3.5 residues, resulting in slight winding, or twist, around the other polypeptide, forming a coiled coil. a about us privacy policy terms of use careers heln contact us
a-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. е g b С d a f f d a С е Identify the three true statements about the structure of keratin Ile-Lys-Asn-Leu-Asn- Glu-Thr is a likely repeat in the a helix of keratin. Glu-Leu-Thr-Asn-Thr-Lys-Cys is a likely repeat in the a helix of keratin. Keratin molecules are very strong due to hydrophilic interactions between charged amino acid side chains. The residues at positions b and c are less likely to be polar or charged because they are in contact with the solvent. The a helix of the coiled coil is wound less tightly than predicted for an a helix oa-Keratin is rich in Cys residues, enabling the formation of covalent cross-links between peptide chains and increasing the strength of the protein. Each polypeptide in the dimer has 3.6 residuess per turn, and a nonpolar group occurs every 3.5 residues, resulting in slight winding, or twist, around the other polypeptide, forming a coiled coil. a about us privacy policy terms of use careers heln contact us
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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Identify three true statments about the structure of keratin
Transcribed Image Text:a-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.
е
g
b
С
d
a
f
f
d
a
С
е
Transcribed Image Text:Identify the three true statements about the structure of keratin
Ile-Lys-Asn-Leu-Asn- Glu-Thr is a likely repeat in the a helix of keratin.
Glu-Leu-Thr-Asn-Thr-Lys-Cys is a likely repeat in the a helix of keratin.
Keratin molecules are very strong due to hydrophilic interactions between charged amino acid side chains.
The residues at positions b and c are less likely to be polar or charged because they
are in contact with the solvent.
The a helix of the coiled coil is wound less tightly than predicted for an a helix
oa-Keratin is rich in Cys residues, enabling the formation of covalent cross-links between peptide chains and
increasing the strength of the protein.
Each polypeptide in the dimer has 3.6 residuess per turn, and a nonpolar group occurs every 3.5 residues, resulting in
slight winding, or twist, around the other polypeptide, forming a coiled coil.
a
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