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 durability Silk resists stretching because of its ẞ conformation ○ The polypeptides in a-keratin are mainly in the a-helical conformation
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- Match each of the statements Collagen Silk fibroid KeratinCompare 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.
- 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.Match each of the statements below with the fibrous protein that mostly fits the description. Coiled-coil of alpha helices V [ Choose] Collagen Silk fibroin Keratin Triple helical arrangement of polypeptide chains Extended anti-parallel beta sheets [ Choose ] Characterized by a predominant (GSGAGA)n repeat in the primary seguence [ Choose] Found in hair, feathers, scales, and nails [ Choose ] Is produced by insects and spiders [ Choose ] The sequence Gly-Pro-Hyp occurs frequently in this fibrous protein [ Choose ] Is characterized by the heptad pseudo- [ Choose ] repeat Major component of skin, tendons, ligaments and teeth [ Choose ] Characterized by regular inter-sheet spacing [ Choose ] of 0.35 and 0.57 nm
- 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?Explain why a-keratins that have many disulfide bondsbetween adjacent polypeptide chains are much less elasticand much harder than those without disulfide bonds.Which of the following statements differentiates structurally albumin (a globular protein) structurally with that of collagen (fibrous protein)? O Peptide bonds in collagen are rigid and fixed, while the peptide bonds in albumin can freely rotate O Collagen possess an elongated shape while albumin resemble a spherical shape The amino acids in albumin are in the L-form while the amino acids in collagen are in the D-form Albumin possess less diverse set of amino acids while collagen can contain a variety of amino acid types