stretch of hydrophobic amino acids
A stretch of hydrophobic amino acids refers to a consecutive sequence of amino acids within a protein that have hydrophobic properties. Hydrophobic amino acids tend to repel water and are often found buried within the interior of a protein structure, away from the surrounding aqueous environment. This characteristic allows them to contribute to the stability of the protein’s folded conformation.
The primary hydrophobic amino acids are:
- Alanine (Ala, A)
- Valine (Val, V)
- Leucine (Leu, L)
- Isoleucine (Ile, I)
- Phenylalanine (Phe, F)
- Tryptophan (Trp, W)
- Methionine (Met, M)
These hydrophobic amino acids are often found in the interior of proteins, where they can form hydrophobic interactions with each other, stabilizing the protein’s folded structure. Such stretches of hydrophobic amino acids are commonly found in the core of globular proteins, where they contribute to the protein’s overall stability.
The presence and arrangement of hydrophobic amino acids within a protein sequence can be crucial for its function, as they can influence protein folding, stability, and interactions with other molecules.