Integral membrane proteins are anchored in lipid bilayers. Which of the following groups of amino acid residues would likely be found in the portion that crosses the lipid bilayer? Nonpolar Polar Acidic Charged

Human Anatomy & Physiology (11th Edition)
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Author:Elaine N. Marieb, Katja N. Hoehn
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Chapter1: The Human Body: An Orientation
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**Question:**

Integral membrane proteins are anchored in lipid bilayers. Which of the following groups of amino acid residues would likely be found in the portion that crosses the lipid bilayer?

**Options:**

- Nonpolar

- Polar

- Acidic

- Charged

**Explanation:**

In the context of integral membrane proteins crossing the lipid bilayer, the amino acid residues that are most likely to be found in these regions are nonpolar. This is because the lipid bilayer itself is hydrophobic (water-repelling) in nature, especially within the core. Nonpolar amino acids, which are also hydrophobic, are more compatible with this environment, allowing the protein to embed itself snugly within the membrane without disrupting the lipid environment. On an educational platform, students might be taught the significance of protein-lipid interactions and the role of hydrophobic forces in membrane protein structure and function.
Transcribed Image Text:**Question:** Integral membrane proteins are anchored in lipid bilayers. Which of the following groups of amino acid residues would likely be found in the portion that crosses the lipid bilayer? **Options:** - Nonpolar - Polar - Acidic - Charged **Explanation:** In the context of integral membrane proteins crossing the lipid bilayer, the amino acid residues that are most likely to be found in these regions are nonpolar. This is because the lipid bilayer itself is hydrophobic (water-repelling) in nature, especially within the core. Nonpolar amino acids, which are also hydrophobic, are more compatible with this environment, allowing the protein to embed itself snugly within the membrane without disrupting the lipid environment. On an educational platform, students might be taught the significance of protein-lipid interactions and the role of hydrophobic forces in membrane protein structure and function.
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