Question

Why are integral membrane proteins difficult to study?

1) They are difficult to isolate in soluble form due to their hydrophobic transmembrane domains.
2) They are difficult to isolate in soluble form due to their hydrophilic transmembrane domains.
3) They are so small.
4) They are so large.
5) None of these are correct.

Answer 1

Integral membrane proteins are difficult to study because their hydrophobic transmembrane domains make them hard to isolate in a soluble form, as they are embedded in the hydrophobic interior of the lipid bilayer and are tightly anchored.

Step-by-step explanation:

Integral membrane proteins are difficult to study because they have hydrophobic transmembrane domains that interact with the hydrophobic interior of the lipid bilayer.

This makes them difficult to isolate in soluble form. Integral proteins are integrated completely into the membrane structure, typically with hydrophobic membrane-spanning regions and hydrophilic regions that either protrude from the membrane or face the cytosol or cell exterior.

Their hydrophobic regions interact strongly with the fatty acid interior of membranes, anchoring them firmly and making their isolation challenging without disrupting their structure and function.