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Answer:
D. In the interior of the folded protein, away from water, or in a transmembrane portion interacting with lipid fatty acid chains.
In a normal protein, it is expected to find valine in the interior of the folded protein, away from water, or in a transmembrane portion, interacting with lipid fatty acid chains (Option D).
Aminoacids can contain hydrophilic side chains that interact with water molecules or hydrophobic side chains that cannot make hydrogen bonds and therefore do not interact with water.
In membrane protein, hydrophilic amino acids are arranged so they can interact with water on the surface of the cell membrane,
Moreover, hydrophobic amino acids of membrane proteins are arranged away from water so they can interact with fatty acid chains in the transmembrane portion of transmembrane proteins or with other hydrophobic amino acids in the interior of the folded protein.
In conclusion, in a normal protein, it is expected to find valine in the interior of the folded protein, away from water, or in a transmembrane portion, interacting with lipid fatty acid chains (Option D).
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