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Hydrophobic amino acids on lipid bi-layer

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12y ago
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5mo ago

Membrane proteins have hydrophobic regions that interact poorly with water molecules, making them insoluble in water. The hydrophobic amino acid residues in these proteins tend to aggregate together to minimize their contact with water, leading to membrane proteins being more stable and functional in lipid bilayers rather than in aqueous solutions.

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Q: Why are membrane proteins are not very soluble in water?
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