How to use this table
- Residue masses are the masses of each amino acid within a chain, after losing water to form peptide bonds. To get a peptide's mass, add the residue masses and then one water (18.01056 Da monoisotopic, 18.0153 Da average), or use the peptide mass calculator.
- Leucine and isoleucine have identical masses, so a basic mass measurement can't tell them apart.
- Side-chain pKa values are typical textbook values for free amino acids. In peptides they shift with neighbouring residues and conditions, and published sets differ slightly.
- Hydropathy uses the Kyte–Doolittle scale: positive values are hydrophobic, negative values hydrophilic. In reverse-phase HPLC, more hydrophobic peptides generally elute later. See How to read an HPLC chromatogram.
- Glycine is the only standard amino acid that isn't chiral. All the others exist in L and D forms; see D-amino acids and peptidomimetics.
Sources and further reading
- Kyte J, Doolittle RF. A simple method for displaying the hydropathic character of a protein. J Mol Biol 1982;157:105–132. doi:10.1016/0022-2836(82)90515-0 · PMID: 7108955
- Steen H, Mann M. The ABC’s (and XYZ’s) of peptide sequencing. Nat Rev Mol Cell Biol 2004;5:699–711. doi:10.1038/nrm1468 · PMID: 15340378