Final answer:
A protein can be embedded on the cytosolic side of the membrane by employing a hydrophobic α helix option 1, which anchors the protein in the hydrophobic interior of the membrane.
Step-by-step explanation:
A protein can be embedded on the cytosolic side of the membrane bilayer by employing a hydrophobic α helix. This is because integral membrane proteins have hydrophobic helical domains that anchor them within the hydrophobic interior of the membrane bilayer. The hydrophobic α helix interacts with the lipid tails of the phospholipid bilayer, allowing the protein to be securely embedded in the membrane. The hydrophilic parts of the protein generally face the aqueous solutions, either the cytosol or the extracellular fluid, depending on the orientation of the protein.
Some integral proteins may span the membrane multiple times and are composed of both hydrophilic and hydrophobic domains. These proteins can create pores for the transport of polar molecules and ions, or they might play a structural role in maintaining cell shape or cell-to-cell connections. The arrangement of hydrophobic regions adjacent to the phospholipid tails and hydrophilic regions protruding from the membrane ensures proper protein placement and function. This orientation is critical for the protein's activity, including cell signaling, substance transport, or cell adhesion.