| AA | Code | Fullname | Side chain type | Mass | pI | pK1(a-COOH) | pK2(a-+NH3) | pKr (R) | hydrophobic | positive | negative | polar | charged | small | tiny | aromatic | aliphatic | van der Waals volume | Remarks
|
| A | Ala | Alanine | hydrophobic | 89.09 | 6.11 | 2.35 | 9.87 | | X | - | - | - | - | X | X | - | - | 67 |
|
| C | Cys | Cysteine | "hydrophobic (Nagano, 1999)" | 121.16 | 5.05 | 1.92 | 10.7 | 8.37 | X | - | - | - | - | X | - | - | - | 86 | "Under oxidizing conditions, two cysteines can join together by a disulfide bond to form the amino acid cystine. When cysteines are part of a protein, insulin for example, this enforces tertiary structure."
|
| D | Asp | Aspartic acid | acidic | 133.1 | 2.85 | 1.99 | 9.9 | 3.9 | - | - | X | X | X | X | - | - | - | 91 |
|
| E | Glu | Glutamic acid | acidic | 147.13 | 3.15 | 2.1 | 9.47 | 4.07 | - | - | X | X | X | - | - | - | - | 109 |
|
| F | Phe | Phenylalanine | hydrophobic | 165.19 | 5.49 | 2.2 | 9.31 | | X | - | - | - | - | - | - | X | - | 135 |
|
| G | Gly | Glycine | hydrophilic | 75.07 | 6.06 | 2.35 | 9.78 | | X | - | - | - | - | X | X | - | - | 48 | "Because of the two hydrogen atoms at the a carbon, glycine is not optically active."
|
| H | His | Histidine | basic | 155.16 | 7.6 | 1.8 | 9.33 | 6.04 | X | X | - | X | X | - | - | X | - | 118 | "In even slightly acidic conditions protonation of the nitrogen occurs, changing the properties of histidine and the polypeptide as a whole. It is used by many proteins as a regulatory mechanism, changing the conformation and behavior of the polypeptide in acidic regions such as the late endosome or lysosome."
|
| I | Ile | Isoleucine | hydrophobic | 131.17 | 6.05 | 2.32 | 9.76 | | - | X | - | X | X | - | - | - | - | 135 |
|
| K | Lys | Lysine | basic | 146.19 | 9.6 | 2.16 | 9.06 | 10.54 | X | - | - | - | - | - | - | - | X | 124 |
|
| L | Leu | Leucine | hydrophobic | 131.17 | 6.01 | 2.33 | 9.74 | | X | - | - | - | - | - | - | - | X | 124 |
|
| M | Met | Methionine | hydrophobic | 149.21 | 5.74 | 2.13 | 9.28 | | X | - | - | - | - | - | - | - | - | 124 | Always the first amino acid to be incorporated into a protein; sometimes removed after translation.
|
| N | Asn | Asparagine | hydrophilic | 132.12 | 5.41 | 2.14 | 8.72 | | - | - | - | X | - | X | - | - | - | 96 |
|
| P | Pro | Proline | hydrophobic | 115.13 | 6.3 | 1.95 | 10.64 | | - | - | - | - | - | X | - | - | - | 90 | Can disrupt protein folding structures like a helix or ß sheet.
|
| Q | Gln | Glutamine | hydrophilic | 146.15 | 5.65 | 2.17 | 9.13 | | - | - | - | X | - | - | - | - | - | 114 |
|
| R | Arg | Arginine | basic | 174.2 | 10.76 | 1.82 | 8.99 | 12.48 | - | X | - | X | X | - | - | - | - | 148 |
|
| S | Ser | Serine | hydrophilic | 105.09 | 5.68 | 2.19 | 9.21 | | - | - | - | X | - | X | X | - | - | 73
|
| T | Thr | Threonine | hydrophilic | 119.12 | 5.6 | 2.09 | 9.1 | | X | - | - | X | - | X | - | - | - | 93
|
| V | Val | Valine | hydrophobic | 117.15 | 6 | 2.39 | 9.74 | | X | - | - | - | - | X | - | - | X | 105
|
| W | Trp | Tryptophan | hydrophobic | 204.23 | 5.89 | 2.46 | 9.41 | | X | - | - | X | - | - | - | X | - | 163
|
| Y | Tyr | Tyrosine | hydrophobic | 181.19 | 5.64 | 2.2 | 9.21 | 10.46 | X | - | - | X | - | - | - | X | - | 141
|