Question

The chemical structure of glycophorin A, the major integral protein of the ___________ ____________ membrane, shows that 17 of 20 amino acids in the _________ helix have hydrophobic side chains

Answer 1

Glycophorin A is an integral protein of the red blood cell membrane, with an alpha-helix that has 17 out of 20 hydrophobic amino acids, allowing it to anchor in the lipid bilayer and function in preventing cell aggregation.

Step-by-step explanation:

The chemical structure of glycophorin A, the major integral protein of the red blood cell membrane, shows that 17 of 20 amino acids in the alpha-helix have hydrophobic side chains. Integral membrane proteins such as glycophorin A are critical for cellular function, because their hydrophobic helical domain anchors them in the lipid bilayer of the membrane, allowing their hydrophilic domains to interact with intracellular or extracellular molecules. This structural characteristic is pivotal for the protein's function in preventing red blood cell aggregation and for other membrane proteins to participate in various cellular processes.