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The lack of polarity means they have no way to interact with highly polar water molecules, making them water fearing.
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Hydrophobic amino acids have little or no polarity in their side chains. How do you know if an amino acid is hydrophobic? Polar amino acid residues have a tendency to be on the outside of a protein, due to the hydrophilic properties of the side chain. Are all polar amino acids hydrophilic?Īll polar amino acids have either an OH or NH2 group (when in aqueous environment), and can therefore make hydrogen bonds with other suitable groups. Where are hydrophilic amino acids found?īecause the charged and polar amino acids are hydrophilic, they are usually found at the surface of a water-soluble protein, where they not only contribute to the solubility of the protein in water but also form binding sites for charged molecules. The hydrophobic amino acids include alanine (Ala, A), valine (Val, V), leucine (Leu, L), isoleucine (Ile, I), proline (Pro, P), phenylalanine (Phe, F) and cysteine (Cys).
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For discussion of OH−π, and CH−O types of hydrogen bonds see Scheiner et al., 2002.
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