How do hydrophobic and hydrophilic residues arrange
themselves in globular proteins?
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Answer / Javed Khan
In globular proteins, hydrophobic residues (e.g., alanine, valine, leucine) tend to be located on the interior of the protein molecule, away from water, due to their preference for nonpolar environments. Hydrophilic residues (e.g., aspartic acid, glutamic acid, lysine, arginine) are typically found on the surface or in contact with water because they are polar and charged.
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