Final answer:
Lipid-anchored proteins remain attached to the membrane via hydrophobic interactions, while peripheral membrane proteins attach through hydrogen bonding and electrostatic forces with polar parts of the membrane.
Step-by-step explanation:
Lipid-anchored proteins interact with the fatty acid interior of the cell membrane through their hydrophobic domains. These proteins remain attached to the membrane since the hydrophobic regions of both the proteins and the lipids in the membrane repel water and preferentially interact with each other, creating a strong non-covalent bond.
Peripheral membrane proteins associate with the cell membrane more loosely compared to lipid-anchored proteins. They attach to the membrane through non-covalent interactions such as hydrogen bonding and electrostatic forces with the polar head groups of the lipids or with integral proteins. These interactions are typically hydrophilic, which allows the peripheral proteins to temporarily associate with the membrane, facilitating functions such as cell signaling, enzymatic activity, and forming part of the cell's recognition sites.