Question

If a protein is supposed to have multiple transmembrane domains (ex: G-Protein Coupled Receptors have 7), how does this system integrate all of these domains?

Answer 1

Proteins with multiple transmembrane domains integrate them through their structure and folding. Transmembrane domains consist of helical regions that span the cell membrane, interacting with the lipid bilayer. These domains work together to create a stable protein structure.

Step-by-step explanation:

Proteins with multiple transmembrane domains, such as G-Protein Coupled Receptors (GPCRs), integrate all of these domains through their structure and folding. Each transmembrane domain consists of a helical region that spans the lipid bilayer of the cell membrane. These helices are typically hydrophobic in nature, allowing them to interact with the hydrophobic interior of the membrane. The multiple transmembrane domains work together to create a stable and functional protein structure, with the extracellular and intracellular domains positioned appropriately for ligand binding and signal transduction.