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The chemical structures of Group II amino acids are:
However, most have at least one atom ( nitrogen, oxygen, or sulfur) with electron pairs available for hydrogen bonding to water and other molecules. The side chains in this group possess a spectrum of functional groups. Group II amino acids are serine, cysteine, threonine, tyrosine, asparagine, and glutamine. Tryptophan contains an indole ring attached to the alanyl side chain. Methionine also provides methyl groups for metabolism. Methionine plays a central role in protein biosynthesis ( translation) as it is almost always the initiating amino acid. Methionine is one of the two amino acids that possess a sulfur atom. (Strictly speaking, this means that proline is not an amino acid but rather an α-imino acid.) Phenylalanine, as the name implies, consists of a phenyl group attached to alanine. Instead, its side chain forms a cyclic structure as the nitrogen atom of proline is linked to two carbon atoms.
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Proline is unique among the standard amino acids in that it does not have both free α-amino and free α-carboxyl groups. Isoleucine is an isomer of leucine, and it contains two chiral carbon atoms. The chemical structures of Group I amino acids are: In aqueous solutions, globular proteins will fold into a three-dimensional shape to bury these hydrophobic side chains in the protein interior. This makes them hydrophobic (“water fearing”).
The R groups of these amino acids have either aliphatic or aromatic groups. Group I amino acids are glycine, alanine, valine, leucine, isoleucine, proline, phenylalanine, methionine, and tryptophan. One of the most useful manners by which to classify the standard (or common) amino acids is based on the polarity (that is, the distribution of electric charge) of the R group (e.g., side chain).
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High-frequency mutation of the TP53 tumor suppressor gene is observed in multiple human cancers, which promotes cancer progression.
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