Identify the three true statements about the structure of keratin. 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. a-Keratin is rich in Cys residues, enabling the formation of covalent cross-links between peptide chains and increasing the strength of the protein. The a helix of the coiled coil is wound less tightly than predicted for an a helix. Asp-Ala-Asp-Ser-Asp-Glu-Glu 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. Val-Glu-Ser-Ala-Ser-Asp-Asp is a likely repeat in the a helix of keratin. ↑ MeeBook Pro

Human Anatomy & Physiology (11th Edition)
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Chapter1: The Human Body: An Orientation
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Identify the three true statements about the structure of keratin.
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.
a-Keratin is rich in Cys residues, enabling the formation of covalent cross-links between peptide chains and increasing
the strength of the protein.
The a helix of the coiled coil is wound less tightly than predicted for an a helix.
Asp-Ala-Asp-Ser-Asp-Glu-Glu 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.
Val-Glu-Ser-Ala-Ser-Asp-Asp is a likely repeat in the a helix of keratin.
↑
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Transcribed Image Text:Identify the three true statements about the structure of keratin. 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. a-Keratin is rich in Cys residues, enabling the formation of covalent cross-links between peptide chains and increasing the strength of the protein. The a helix of the coiled coil is wound less tightly than predicted for an a helix. Asp-Ala-Asp-Ser-Asp-Glu-Glu 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. Val-Glu-Ser-Ala-Ser-Asp-Asp is a likely repeat in the a helix of keratin. ↑ MeeBook Pro
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