AP BIOLOGY

THE CELL

STRUCTURE AND FUNCTION OF THE CELL

Question [CLICK ON ANY CHOICE TO KNOW THE RIGHT ANSWER]
Why do integral proteins have mainly nonpolar amino acids in their structure?
A
So that they can allow water to pass through
B
So they can anchor themselves and span the hydrophobic core of cell membrane
C
So that they are not repelled by the phosphate heads
D
To form active sites for ATP hydrolysis
Explanation: 

Detailed explanation-1: -In other words, an integral protein locks itself into the cellular membrane. It does so with regions of specific amino acids which are attracted to the middle of the plasma membrane.

Detailed explanation-2: -Small nonpolar molecules, such as O2 and CO2, are soluble in the lipid bilayer and therefore can readily cross cell membranes. Small uncharged polar molecules, such as H2O, also can diffuse through membranes, but larger uncharged polar molecules, such as glucose, cannot.

Detailed explanation-3: -Integral proteins are those that are permanently attached to the membrane via stabilizing hydrophobic interactions. Remember that the membrane core consists of hydrocarbon tails and therefore non-polar interactions will stabilize the attachment of the protein within the membrane.

Detailed explanation-4: -The portions of an integral membrane protein found inside the membrane are hydrophobic, while those that are exposed to the cytoplasm or extracellular fluid tend to be hydrophilic.

There is 1 question to complete.