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Each amino acid is composed of a central carbon atom (the alpha carbon) bonded to an amino group (-NH2), a carboxyl group (-COOH), a hydrogen atom (H), and a side chain (R-group) that is unique to each amino acid. The R-group gives each amino acid its unique chemical properties. Some amino acids are nonpolar, while others are polar, positively charged, or negatively charged. These properties influence how the protein folds and interacts with other molecules in the cell. The sequence of amino acids in a polypeptide chain determines the protein's primary structure. The primary structure then influences the formation of the secondary structure, which includes alpha helices and beta sheets. The secondary structure folds into a tertiary structure, a complete three-dimensional shape of the protein. Furthermore, several polypeptide chains may come together to form the quaternary structure. These various structural levels contribute to the final protein shape, which is directly related to its function.
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