Which statement is false?○ Each chain of collagen adopts a right-handed helix○ Disulfide linkages modulate the properties of keratin structure.O Modified lysine residues can enhance collagen's durabilitySilk resists stretching because of its ẞ conformation○ The polypeptides in a-keratin are mainly in the a-helical conformation

Step 1: The false statement is : Silk resists stretching because of its β conformation.…

Answered: Which statement is false? ○ Each chain…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Similar questions

Match each of the statements Collagen Silk fibroid Keratin
Compare and contrast structural features of collagen and α-keratin (OK to do this as a list or table comparing/contrasting 3-4 points, e.g. type of helices, noncovalent and covalent interactions between helices, favored residues). Can you please help?
What could be the reason why hydroxylation of proline residues is critical to the structural integrity of collagen? Select the correct response The hydroxyl moities in Pro form disulfide bonds which stabilize collagen structure. The hydroxyl moities in Pro form ionic bonds (salt bridges) which stabilize collagen structure. The hydroxyl moities in Pro form hydrophobic interactions which stabilize collagen structure. The hydroxyl moities in Pro form peptide bonds which stabilize collagen structure. The hydroxyl moities in Pro form H-bonds which stabilize collagen structure.
Which of the following statements is true O Sphingomyelin posses phosphoryl serine in addition to two long hydrocarbon chains, one contributed by a fatty acid and the other by sphingosine OLipid compositions of membrane mono-layers are symmetrical O Unsaturated fatty acids have double bond(s) in the cis configuration In ABO blood typing, lack of glycosyltransferase and galactosyltransferase produces AB blood group
Both a-keratin and collagen are fibrous proteins.however,the hydrogen bonding pattern is different between the helices of the respective proteins.what os the major difference?
α‑Keratin is an intermediate filament with a basic structural unit of two α helices in a coiled coil. Each helix has a seven‑residue repeating unit (heptad repeat). A representation of the α helices of a coiled coil dimer is shown. Each letter represents a different amino acid residue.
Peptide bonds are the last bonds to break when collagen proteins are denatured Select one: of O True O False Estion
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…
3
The core of pectin molecules is a polymer of a (1®4)-linked D-galacturonate. Draw one of its residues.
What in the world is this?
After the peptide chain of collagen has been formed, many of the proline residues are hydroxylated on one of the ring carbon atoms. Why is this process important for the triple helix of collagen?

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