Glycine, alanine, valine, leucine, isoleucine, and proline are considered amino acids with nonpolar aliphatic side chains. Which of these amino acids are often observed on the surface of protein?
Glycine and proline
Amino acids with nonpolar aliphatic side chains tend to be hydrophobic and are generally found buried in the interior of proteins where they can interact with other hydrophobic amino acids via van der Waals interactions. These amino acids are not usually found on the surface of proteins where they would be exposed to the aqueous environment and would have to interact with water molecules. However, in some cases, these amino acids can be found on the surface of proteins, especially in regions of the protein that are involved in interacting with other hydrophobic surfaces, or in proteins that require a hydrophobic surface to be functionally active.
Out of the amino acids listed, glycine and proline are often observed on the surface of proteins. Glycine is the smallest amino acid and lacks a side chain, making it very flexible and able to adopt a variety of conformations, even on the surface of proteins. Proline has a rigid, cyclic structure that can be accommodated on the surface of proteins. While alanine, valine, leucine, and isoleucine are less commonly found on the surface due to their larger and more rigid side chains.
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