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Coiled-coils are typically found in proteins that require an elongated structural framework. Which of the following proteins do you expect to have a coiled-coil domain?

(a) insulin
(b) collagen
(c) myoglobin
(d) porin

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Final answer:

Collagen is the protein that typically has a coiled-coil domain due to its triple-helix structure, which provides an elongated structural framework in connective tissues. Insulin, myoglobin, and porin do not have this type of structure.

Step-by-step explanation:

You've asked which protein you would expect to have a coiled-coil domain. Among the options provided, collagen is the protein that has a triple-helix, which is a specific type of coiled-coil structure. Collagen provides an elongated structural framework essential in connective tissues.

Now let's briefly explore why the other options are not typically associated with coiled-coil domains:

  • Insulin is a hormone that regulates glucose levels and does not have a coiled-coil domain.
  • Myoglobin is a protein that stores oxygen in muscle cells and has a globular structure rather than an elongated coiled-coil.
  • Porin is a membrane protein forming pores and does not have a typical coiled-coil structure as it is not primarily a fibrous protein.

Remember, the shape and structure of a protein are critical to its function. Fibrous proteins like collagen are strong, durable, and usually hydrophobic because of their elongated shape and the structural stability provided by the coiled-coil domain.

User Alexander Leithner
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