Question

the same protein interacts with both the external and internal environments of the cell. this graphic uses different - colored blobs to represent membrane proteins and the cartoon way of drawing phospholipids to highlight the three locations: outside of cell inside of cell proteins on the inside or outside of the phospholipid bilayer are called peripheral membrane proteins; proteins that span the bilayer are called transmembrane membrane proteins and are part of a category called integral membrane proteins. these names are descriptive: peripheral membrane proteins are on the periphery and integral membrane proteins are integrated into the bilayer. what stabilizes the phospholipid bilayer in a cell membrane? (this is another way of asking, why does a phospholipid bilayer exist?) select all that apply. hydrophobic interactions among the tails on phospholipids hydrogen bonding between hydrophilic heads on phospholipids and water molecules inside the cell. hydrogen bonding between water molecules inside or outside the cell and polar or charged r - groups on proteins at the cell surface (either interior or exterior). hydrogen bonding between hydrophilic heads on phospholipids and water molecules outside the cell. hydrophobic interactions between the tails on phospholipids and nonpolar r - groups on membrane proteins.

Explanation:

Phospholipids have hydrophilic heads and hydrophobic tails. Hydrophobic tails interact with each other and with non - polar R - groups on membrane proteins, while hydrophilic heads form hydrogen bonds with water molecules inside and outside the cell. These interactions stabilize the bilayer structure. Hydrogen bonding between water and protein R - groups is not directly related to bilayer stability.

Answer:

Hydrophobic interactions among the tails on phospholipids
Hydrogen bonding between hydrophilic heads on phospholipids and water molecules inside the cell
Hydrogen bonding between hydrophilic heads on phospholipids and water molecules outside the cell
Hydrophobic interactions between the tails on phospholipids and nonpolar R - groups on membrane proteins