Question

Porin proteins-which form large, water-filled pores in mitochondrial and

bacterial membranes-fold into /beta barrel structures. The amino acids that face
the outside of the barrel have what kind of side chains?
A. Hydrophilic
B. Hydrophobic

Answer 1

The amino acids on the outside of the β-barrel structure of porin proteins have hydrophobic side chains, which allow the proteins to interact with the phospholipid membrane.

Step-by-step explanation:

Porin proteins form large, water-filled pores in mitochondrial and bacterial membranes and fold into β-barrel structures. The amino acids that face the outside of the barrel have hydrophobic side chains. These hydrophobic amino acids interact with the hydrocarbon tails of the phospholipids within the membrane. In contrast, hydrophilic amino acids face the interior of the pore, where they can interact with water and ions that pass through the channel. This arrangement facilitates the function of the porin as a channel while maintaining the integrity of the cell membrane.