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Amino Acids Reference Chart

Types of Amino Acids

Amino AcidReagentCell Culture & Molecular BiologyAnalytical & Sensitive Applications
Alanine (Ala/A)A7627A746905129
Arginine (Arg/R)A5006A809411009
Asparagine (Asn/N)A8381A4284A7094
Aspartic acid (Asp/D)A9256A7219A8949
Cysteine (Cys/C)C7880C685230129
 C7352 
Glutamic acid (Glu/E)G1251G841549449
Glutamine (Gln/Q)G3126G854049419
 G7513 
Glycine (Gly/G)G7126G889850046
Histidine (His/H)H8000H603453319
Hydroxyproline (Hyp/O)H54409H5534 
Isoleucine (Ile/I)I2752I740358879
Leucine (Leu/L)L8000L891261819
Lysine (Lys/K)L5626L866262929
Methionine (Met/M)M9625M530864319
Phenylalanine (Phe/F)P2126P5482 
Proline (Pro/P)P0380P560781709
Serine (Ser/S)S4500S431184959
Threonine (Thr/T)T8625T844189179
Tryptophan (Trp/W)T0254T894193659
Tyrosine (Tyr/Y) T856693829
 T1145 
Valine (Val/V)V0500V051394619

Properties of Common Amino Acids

NameMolecular
Weight
Molecular
Formula
Residue
Formula
Residue Weight
(-H2O)
pKa1pKb2pKx3pl4
Alanine (Ala/A)89.10C3H7NO2C3H5NO71.082.349.696.00
Arginine (Arg/R)174.20C6H14N4O2C6H12N4O156.192.179.0412.4810.76
Asparagine (Asn/N)132.12C4H8N2O3C4H6N2O2114.112.028.805.41
Aspartic acid (Asp/D)133.11C4H7NO4C4H5NO3115.091.889.603.652.77
Cysteine (Cys/C)121.16C3H7NO2SC3H5NOS103.151.9610.288.185.07
Glutamic acid (Glu/E)147.13C5H9NO4C5H7NO3129.122.199.674.253.22
Glutamine (Gln/Q)146.15C5H10N2O3C5H8N2O2128.132.179.135.65
Glycine (Gly/G)75.07C2H5NO2C2H3NO57.052.349.605.97
Histidine (His/H)155.16C6H9N3O2C6H7N3O137.141.829.176.007.59
Hydroxyproline (Hyp/O)131.13C5H9NO3C5H7NO2113.111.829.65
Isoleucine (Ile/I)131.18C6H13NO2C6H11NO113.162.369.606.02
Leucine (Leu/L)131.18C6H13NO2C6H11NO113.162.369.605.98
Lysine (Lys/K)146.19C6H14N2O2C6H12N2O128.182.188.9510.539.74
Methionine (Met/M)149.21C5H11NO2SC5H9NOS131.202.289.215.74
Phenylalanine (Phe/F)165.19C9H11NO2C9H9NO147.181.839.135.48
Proline (Pro/P)115.13C5H9NO2C5H7NO97.121.9910.606.30
Pyroglutamatic (Glp/U)139.11C5H7NO3C5H5NO2121.095.68
Serine (Ser/S)105.09C3H7NO3C3H5NO287.082.219.155.68
Threonine (Thr/T)119.12C4H9NO3C4H7NO2101.112.099.105.60
Tryptophan (Trp/W)204.23C11H12N2O2C11H10N2O186.222.839.39
5.89
Tyrosine (Tyr/Y)181.19C9H11NO3C9H9NO2163.182.209.1110.075.66
Valine (Val/V)117.15C5H11NO2C5H9NO99.132.329.625.96

pKa is the negative of the logarithm of the dissociation constant for the -COOH group.
2 pKb is the negative of the logarithm of the dissociation constant for the -NH3 group.
3 pKx is the negative of the logarithm of the dissociation constant for any other group in the molecule.
4 pl is the pH at the isoelectric point.
Reference: D.R. Lide, Handbook of Chemistry and Physics72nd Edition, CRC Press, Boca Raton, FL, 1991.


Amino Acids by Side Chain

Amino acids are the compounds or building blocks that make up peptides and proteins. Each amino acid is structured from an amino group and a carboxyl group bound to a tetrahedral carbon. This carbon is designated as the α-carbon (alpha-carbon). 

Amino acids differ from each other with respect to their side chains, which are referred to as R groups. The R group for each of the amino acids will differ in structure, electrical charge, and polarity.

Refer to the charts and structures below to explore amino acid properties, types, applications, and availability.


Amino Acids with Hydrophobic Side Chain – Aliphatic


Amino Acids with Hydrophobic Side Chain – Aromatic


Amino Acids with Polar Neutral Side Chains


Amino Acids with Electrically Charged Side Chains – Acidic


Amino Acids with Electrically Charged Side Chains – Basic



Hydrophobicity Index for Common Amino Acids

The hydrophobicity index is a measure of the relative hydrophobicity, or how soluble an amino acid is in water. In a protein, hydrophobic amino acids are likely to be found in the interior, whereas hydrophilic amino acids are likely to be in contact with the aqueous environment.

The values in the table below are normalized so that the most hydrophobic residue is given a value of 100 relative to glycine, which is considered neutral (0 value). The scales were extrapolated to residues which are more hydrophilic than glycine.

At pH 2AAt pH 7B
Very Hydrophobic
Leu      100        
Phe      100
Ile100Ile99
Phe92Trp97
Trp84Leu97
Val79Val76
Met74Met74
Hydrophobic
Cys52Tyr63
Tyr49Cys49
Ala47Ala41
Neutral
Thr13Thr13
Glu8His8
Gly0Gly0
Ser-7Ser-5
Gln-18Gln-10
Asp-18  
Hydrophilic
Arg-26Arg-14
Lys-37Lys-23
Asn-41Asn-28
His-42Glu-31
Pro-46Pro-46 (used pH 2)
  Asp-55

ApH 2 values: Normalized from Sereda et al., J. Chrom. 676: 139-153 (1994).
BpH 7 values: Monera et al., J. Protein Sci. 1: 319-329 (1995).

References

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Cho IJ, Ahn JY, Kim S, Choi MS, Ha TY. 2008. Resveratrol attenuates the expression of HMG-CoA reductase mRNA in hamsters. Biochemical and Biophysical Research Communications. 367(1):190-194. https://doi.org/10.1016/j.bbrc.2007.12.140
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Polleux F, Ghosh A. 2002. The Slice Overlay Assay: A Versatile Tool to Study the Influence of Extracellular Signals on Neuronal Development. Science Signaling. 2002(136):pl9-pl9. https://doi.org/10.1126/stke.2002.136.pl9
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Rama Rao KV, Reddy PV, Tong X, Norenberg MD. 2010. Brain Edema in Acute Liver Failure. The American Journal of Pathology. 176(3):1400-1408. https://doi.org/10.2353/ajpath.2010.090756
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Marx M, Günter RH, Hucko W, Radnikow G, Feldmeyer D. 2012. Improved biocytin labeling and neuronal 3D reconstruction. Nat Protoc. 7(2):394-407. https://doi.org/10.1038/nprot.2011.449
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