Amino acids constitute the building blocks of proteins. The 20 different types of amino acids, on the basis of physicochemical attributes, can be classified into three main classes – hydrophilic, hydrophobic and charged.
Hydrophilic amino acids are polar while hydrophobic amino acids are non-polar, this is the main difference between them.
Hydrophobic Amino Acids
- These are the kinds of amino acids having the nature of non-polarity; they fail to interact with water and cannot be dissolved in water
- These include Valine, Alanine, Proline, Phenylalanine and more
- Residues typically can be seen in the protein core, which are separated from the solvent
- It takes part in the van der Waals interactions required to stabilize the structure of proteins
Hydrophilic Amino Acids
- These are the kinds of amino acids having the nature of polarity. It attracts water and is able to dissolve in it, given its nature
- These include Tyrosine, Glutamine, Threonine, Serine, Asparagine
Key Difference between Hydrophobic and Hydrophilic Amino Acids
The table below depicts the difference between Hydrophobic and Hydrophilic Amino Acids.
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These are the amino acids with a nonpolar nature |
These are the amino acids with a polar nature |
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At the centre |
Towards the surface |
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It repels when it interacts with water |
It attracts when it interacts with water |
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Long side chains mostly having hydrogen and carbon atoms |
Has short side chains or side chains with hydrophilic groups |
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Small |
Large |
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Valine, Alanine, Proline, Phenylalanine |
Tyrosine, Glutamine, Threonine, Serine, Asparagine |
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