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A membrane-associated protein is isolated and found to contain multiple alpha helices and a large number of hydrophobic amino acids. This protein is most likely a:

1) Enzyme
2) Transporter
3) Receptor
4) Channel

User MLN
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1 Answer

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Final answer:

The protein with multiple alpha helices and hydrophobic amino acids is most likely functioning as a channel, allowing the selective passage of substances across the cell membrane. The correct answer is option 4.

Step-by-step explanation:

When we consider the characteristics of membrane-associated proteins with multiple alpha helices and a large number of hydrophobic amino acids, we can deduce their likely function in cellular contexts. Proteins that contain such a high proportion of hydrophobic amino acids and alpha-helices are typically involved in spanning the hydrophobic core of cell membranes. These alpha-helices allow the protein to penetrate the membrane, while the hydrophobic amino acids interact with the lipid environment, facilitating the protein’s integration into the membrane.

The reference to hydrophobic alpha helices suggests this protein could be best described as a transmembrane protein. Alpha-helices are often involved in forming channels or pores across the lipid bilayer. Considering these characteristics, such a protein could function as a transporter or channel, creating pores for the movement of polar molecules and ions. While enzymes can indeed associate with membranes, they do not typically span the membrane with alpha-helices in the same way that transporters or channels might. Receptors often span membranes but their primary function lies in signal transduction rather than forming a pore or channel for substances to pass through.

Therefore, the protein described is most likely a channel, which utilizes its hydrophobic traits and structural alpha-helices to facilitate the selective passage of substances across the cell membrane.

The correct option in the final answer is: 4) Channel

User Ben Arent
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