Numbers between parentheses indicate the class number, for a given property. Hydrogen donor or acceptor atom (4 classes) In this approach, nonfluorescent HA reacts with. 26 In this context, amino acids are ideal hydrophobic moieties to drive the amphiphilicity for the formation of NCPDs. IMGT classes of the amino acids side chain properties Hydrophobic amino acids such as tryptophan, phenylalanine, and proline can be conjugated to a hydrophilic polymer to modulate the amphiphilicity of self-assembling nanoparticles. The motifs formed in cocrystals of alpha-amino acids and in crystals of beta- and gamma-amino acids are similar to those of alpha-amino acids. Table 2: IMGT classes of the 20 common amino acids side chain properties. The list of motifs displayed by each structure reveals structural similarities and it can be used to compare polymorphs. (A, C, G, I, L, M, F, P, W, V) amino acids. Regarding the 'Charge', the 'nonpolar' class includes the other 10 uncharged The 'nonpolar' class comprises amino acids without hydrogen donor or acceptor atoms ('none'), and also Includes the 5 charged (R, H, K, D, E) and 5 uncharged (N, Q, S, T, Y) amino acids. Indeed, tryptophan, despite its hydrogen donor atom, has been classified in the IMGT 'nonpolar' class,Īs it participates to the nonpolar core of the structural domains.Regarding the 'Charge', the 'polar' class The 'polar' class comprises amino acids with hydrogen donor and/or acceptor atoms, except tryptophan. Nonpolar: A, C, G, I, L, M, F, P, W, V.There are 4 IMGT 'Hydrogen donor or acceptor atoms' classes.īased on the presence or absence of hydrogen donor and/or acceptor atoms. The sulfhydryl group of cystein and phenolic hydroxyl group of tyrosine show some degree of pH-dependent ionization. Uncharged: A, N, C, Q, G, I, L, M, F, P, S, T, W, Y, V.There are 5 IMGT 'Volume' classes (volume in Å 3).Īmino acids in each class are in the order of Table 2:Īmino acids are ordered from the smallest one (G) to the largest one (W). Has been classified in the IMGT 'hydrophobic' class, as it participates to the hydrophobic core of the structural domains. (1) Tryptophan, despite its value of -0.9 in the Kyte-Doolittle scale, Amino acids are organic compounds containing amine - NH 2 carboxyl -COOH side chain R group The major key elements if amino acids are carbon, hydrogen, nitrogen, oxygen. To the most hydrophilic one, Arginine (R, on the right hand side), according to the Kyte-Doolitle scale. They have been individualized from 'Chemical' (G and P from 'aliphatic', F, W and Y from 'aromatic') classes, based on the structural properties of the amino acids in protein domains.Īmino acids in each class are in the order of Table 2 :Īmino acids are ordered from the most hydrophobic one, Isoleucine (I, on the left hand side) The nine hydrophilic amino acids are listed below, with the remaining two. The nine hydrophobic amino acids are alanine (Ala), glycine (Gly), valine (Val), leucine (Leu), isoleucine (Ile), phenylalanine (Phe), proline (Pro), methionine (Met), and tryptophan (Trp). 'Chemical', 'Charge', 'Hydrogen donor or acceptor atoms'Īnd 'Polarity' properties of the side chains (or R- groups). Of the 20 common amino acids, all are defined by their R group's chain atoms.
The 11 IMGT 'Physicochemical' classes were defined on the 'Hydrophathy', 'Volume', Figure 1: The 11 IMGT 'Physicochemical' classes of the 20 common amino acids.