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.