The following amino acids are considered hydrophobic, meaning they are not attracted to water:
| Amino Acid | Abbreviation |
|---|---|
| Glycine | Gly |
| Alanine | Ala |
| Valine | Val |
| Leucine | Leu |
| Isoleucine | Ile |
| Proline | Pro |
| Phenylalanine | Phe |
| Methionine | Met |
| Tryptophan | Trp |
These nine amino acids share a common characteristic: they have nonpolar side chains. This nonpolarity makes them repel water and cause them to cluster together in aqueous environments. Understanding which amino acids are hydrophobic is crucial in understanding protein folding and structure.
- Why are these amino acids hydrophobic?
- They have side chains composed primarily of carbon and hydrogen atoms.
- These carbon-hydrogen bonds do not form strong attractions to water molecules.
- Therefore, they tend to avoid contact with water.
- How does this affect protein structure?
- Hydrophobic amino acids cluster in the interior of a protein to minimize their contact with water.
- This clustering contributes to the protein's three-dimensional shape and stability.
- Examples
- Valine: As shown in the reference, valine's structure showcases a hydrocarbon side chain, making it nonpolar and hydrophobic.
In essence, the hydrophobic nature of these amino acids is a driving force in protein structure and function.
