Amino acids
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IMGT classes of the 20 common amino acidsCiting this page: Pommié, C. et al., J. Mol. Recognit., 17, 17-32 (2004). PMID: 14872534 IMGT 'Physicochemical' classes of the 20 common amino acidsEleven IMGT 'Physicochemical' classes of the 20 common amino acids have been defined by the physicochemical properties of their side chains (Figure 1) [1]. These standardized classes are used in IMGT® databases and tools, for the description of amino acid class changes in mutations and protein engineering. Figure 1: The 11 IMGT 'Physicochemical' classes of the 20 common amino acids [1]. The 11 IMGT 'Physicochemical' classes were defined on the 'Hydrophathy', 'Volume', 'Chemical', 'Charge', 'Hydrogen donor or acceptor atoms' and 'Polarity' properties of the side chains (or R- groups).
'Hydropathy'There are 3 IMGT 'Hydropathy' classes. Amino acids in each class are in the order of Table 2 :
Amino acids are ordered from the most hydrophobic one, Isoleucine (I, on the left hand side) to the most hydrophilic one, Arginine (R, on the right hand side), according to the Kyte-Doolitle scale [2]. (1) Tryptophan, despite its value of -0.9 in the Kyte-Doolittle scale, has been classified in the IMGT 'hydrophobic' class, as it participates to the hydrophobic core of the structural domains. 'Volume'There are 5 IMGT 'Volume' classes (volume in Å3). Amino acids in each class are in the order of Table 2:
Amino acids are ordered from the smallest one (G) to the largest one (W). 'Chemical'There are 7 'Chemical' classes [1]. Amino acids in each class are in the order of Table 2:
'Charge'There are 3 IMGT 'Charge' classes. Amino acids in each class are in the order of Table 2:
The sulfhydryl group of cystein and phenolic hydroxyl group of tyrosine show some degree of pH-dependent ionization. 'Hydrogen donor or acceptor atoms'There are 4 IMGT 'Hydrogen donor or acceptor atoms' classes. Amino acids in each class are in the order of Table 2:
'Polarity'There are 2 IMGT 'Polarity' classes, based on the presence or absence of hydrogen donor and/or acceptor atoms. Amino acids in each class are in the order of Table 2:
The 'polar' class comprises amino acids with hydrogen donor and/or acceptor atoms, except tryptophan. Indeed, tryptophan, despite its hydrogen donor atom, has been classified in the IMGT 'nonpolar' class, as it participates to the nonpolar core of the structural domains.Regarding the 'Charge', the 'polar' class includes the 5 charged (R, H, K, D, E) and 5 uncharged (N, Q, S, T, Y) amino acids. The 'nonpolar' class comprises amino acids without hydrogen donor or acceptor atoms ('none'), and also includes tryptophan. Regarding the 'Charge', the 'nonpolar' class includes the other 10 uncharged (A, C, G, I, L, M, F, P, W, V) amino acids. Table 2: IMGT classes of the 20 common amino acids side chain properties.
Numbers between parentheses indicate the class number, for a given property. Color menu for the 3 IMGT amino acid 'Hydropathy' classes What are the 4 types of amino acid side chains?There are basically four different classes of amino acids determined by different side chains: (1) non-polar and neutral, (2) polar and neutral, (3) acidic and polar, (4) basic and polar.
What are the three different types of side chains in amino acids?Each amino acid is identical except for its side chain, or R group. It is the charge, shape, polarity, and size of a side chain that gives each amino acid its unique biochemical properties. Amino acid side chains are typically grouped into non-polar, polar, acidic, and basic categories.
How many different types of side chains exist for amino acids?There are 20 different amino acids distinguished by their unique side chains. They range from a simple hydrogen atom (glycine) to a complex 2-ring resonating aromatic system (tryptophan).
What are the 6 polar neutral amino acids?Six amino acids have side chains that are polar but not charged. These are serine (Ser), threonine (Thr), cysteine (Cys), asparagine (Asn), glutamine (Gln), and tyrosine (Tyr).
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