Amino Acid Chart

The Amino Acid Chart is a science reference tool covering amino acid chart, amino acid structure chart, essential amino acids chart, and the 20 amino acids chart. Use the chart below to look up values instantly. Printable and downloadable versions are available on this page.

Amino Acid Chart — All 20 Standard Amino Acids

The 20 Standard Amino Acids — Complete Reference
Amino Acid Name 3-Letter Code 1-Letter Code Chemical Category Side Chain Property Molecular Weight Essential or Non-Essential
AlanineAlaAAliphatic nonpolarSmall hydrophobic side chain89.1 DaNon-essential
ArginineArgRBasic polarPositively charged at physiological pH174.2 DaConditionally essential
AsparagineAsnNPolar unchargedAmide side chain132.1 DaNon-essential
AspartateAspDAcidic polarNegatively charged at physiological pH133.1 DaNon-essential
CysteineCysCPolar unchargedContains sulphur — forms disulphide bonds121.2 DaConditionally essential
GlutamateGluEAcidic polarNegatively charged at physiological pH147.1 DaNon-essential
GlutamineGlnQPolar unchargedAmide side chain — most abundant in blood146.2 DaConditionally essential
GlycineGlyGAliphatic nonpolarSmallest amino acid — no side chain chirality75.0 DaNon-essential
HistidineHisHBasic polarImidazole side chain — buffers near physiological pH155.2 DaEssential
IsoleucineIleIAliphatic nonpolarBranched chain — hydrophobic131.2 DaEssential
LeucineLeuLAliphatic nonpolarBranched chain — most common in proteins131.2 DaEssential
LysineLysKBasic polarPositively charged — modified by acetylation or ubiquitination146.2 DaEssential
MethionineMetMAliphatic nonpolarContains sulphur — universal start codon amino acid149.2 DaEssential
PhenylalaninePheFAromatic nonpolarLarge hydrophobic benzyl side chain165.2 DaEssential
ProlineProPAliphatic nonpolarCyclic side chain — disrupts alpha helices115.1 DaNon-essential
SerineSerSPolar unchargedHydroxyl group — phosphorylation site105.1 DaNon-essential
ThreonineThrTPolar unchargedHydroxyl group — phosphorylation site119.1 DaEssential
TryptophanTrpWAromatic nonpolarLargest amino acid — indole side chain204.2 DaEssential
TyrosineTyrYAromatic polarHydroxyl on benzene ring — phosphorylation and signalling181.2 DaConditionally essential
ValineValVAliphatic nonpolarBranched chain hydrophobic117.1 DaEssential

Source: NCBI — Biochemistry (Berg et al.) and IUPAC amino acid nomenclature

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Essential Amino Acids Chart

Essential amino acids cannot be synthesised by the human body in adequate amounts and must be obtained from dietary protein.

Essential and Conditionally Essential Amino Acids
Classification Amino Acids Key Dietary Sources
Essential (9)
Must come from diet
Histidine, Isoleucine, Leucine, Lysine, Methionine, Phenylalanine, Threonine, Tryptophan, Valine Animal proteins (meat, eggs, dairy), soy protein. All 9 are found in complete proteins.
Conditionally Essential
Required in higher amounts under stress, illness, or growth
Arginine, Cysteine, Glutamine, Tyrosine (and sometimes Glycine, Proline, Serine) Illness, surgery, rapid growth, and extreme exercise increase requirements beyond what the body can synthesise.
Non-essential (11)
Synthesised by the body
Alanine, Asparagine, Aspartate, Glutamate, Glycine, Proline, Serine (and others) The body produces these from other compounds. Dietary intake still contributes.

Source: WHO Protein and Amino Acid Requirements and Institute of Medicine — Dietary Reference Intakes

Amino Acid Structure Categories

Amino Acid Chemical Categories and Properties
Category Amino Acids in This Category Side Chain Property Biological Significance
Nonpolar aliphatic Glycine, Alanine, Valine, Leucine, Isoleucine, Proline, Methionine Hydrophobic — repel water Tend to cluster in the interior of folded proteins away from aqueous environments.
Aromatic Phenylalanine, Tyrosine, Tryptophan Hydrophobic to amphipathic — absorb UV light at 280 nm Protein UV absorbance at 280 nm used to quantify protein concentration in laboratory settings.
Polar uncharged Serine, Threonine, Asparagine, Glutamine, Cysteine, Tyrosine Hydrophilic — hydrogen bond donors and acceptors Common sites for post-translational modifications including phosphorylation and glycosylation.
Positively charged (basic) Lysine, Arginine, Histidine Carry positive charge at physiological pH — bind DNA Found abundantly in histone proteins that package DNA in the nucleus.
Negatively charged (acidic) Aspartate, Glutamate Carry negative charge at physiological pH — repel other negatively charged molecules Active sites of many enzymes. Glutamate is the primary excitatory neurotransmitter in the brain.

Source: NCBI — Biochemistry (Berg et al.)

Amino Acid Single-Letter Code Quick Reference

The single-letter amino acid code is used in protein sequence databases, alignments, and bioinformatics tools — it is worth memorising the most common ones.

Amino Acid Single-Letter Codes — Alphabetical Reference
Letter Code Amino Acid Name Letter Code Amino Acid Name
AAlanineLLeucine
CCysteineMMethionine
DAspartateNAsparagine
EGlutamatePProline
FPhenylalanineQGlutamine
GGlycineRArginine
HHistidineSSerine
IIsoleucineTThreonine
KLysineVValine
WTryptophan
YTyrosine

Amino Acid Reference Tool

Search, filter, and explore all 20 amino acids by name, abbreviation, essential status, polarity, or charge. Click any row to expand its codon list.

20 of 20 amino acids shown
Amino Acid3-Letter1-LetterCategoryMol. WeightEssentialCodons
AlanineAlaAAliphatic nonpolar89.1 DaNon-essentialGCU, GCC, GCA, GCG
ArginineArgRBasic polar174.2 DaConditionally essentialCGU, CGC, CGA, CGG, AGA, AGG
AsparagineAsnNPolar uncharged132.1 DaNon-essentialAAU, AAC
AspartateAspDAcidic polar133.1 DaNon-essentialGAU, GAC
CysteineCysCPolar uncharged121.2 DaConditionally essentialUGU, UGC
GlutamateGluEAcidic polar147.1 DaNon-essentialGAA, GAG
GlutamineGlnQPolar uncharged146.2 DaConditionally essentialCAA, CAG
GlycineGlyGAliphatic nonpolar75.0 DaNon-essentialGGU, GGC, GGA, GGG
HistidineHisHBasic polar155.2 DaEssentialCAU, CAC
IsoleucineIleIAliphatic nonpolar131.2 DaEssentialAUU, AUC, AUA
LeucineLeuLAliphatic nonpolar131.2 DaEssentialUUA, UUG, CUU, CUC, CUA, CUG
LysineLysKBasic polar146.2 DaEssentialAAA, AAG
MethionineMetMAliphatic nonpolar149.2 DaEssentialAUG
PhenylalaninePheFAromatic nonpolar165.2 DaEssentialUUU, UUC
ProlineProPAliphatic nonpolar115.1 DaNon-essentialCCU, CCC, CCA, CCG
SerineSerSPolar uncharged105.1 DaNon-essentialUCU, UCC, UCA, UCG, AGU, AGC
ThreonineThrTPolar uncharged119.1 DaEssentialACU, ACC, ACA, ACG
TryptophanTrpWAromatic nonpolar204.2 DaEssentialUGG
TyrosineTyrYAromatic polar181.2 DaConditionally essentialUAU, UAC
ValineValVAliphatic nonpolar117.1 DaEssentialGUU, GUC, GUA, GUG

Frequently Asked Questions

How many amino acids are there?

There are 20 standard amino acids encoded by the genetic code. Two additional amino acids — selenocysteine and pyrrolysine — are considered the 21st and 22nd amino acids as they are incorporated by specific mechanisms in some organisms.

What are the 9 essential amino acids?

The nine essential amino acids are Histidine, Isoleucine, Leucine, Lysine, Methionine, Phenylalanine, Threonine, Tryptophan, and Valine. They must be obtained from dietary protein because the human body cannot synthesise them in adequate amounts.

What is a complete protein?

A complete protein contains all nine essential amino acids in adequate proportions. Animal proteins (meat, eggs, dairy, fish) are complete proteins. Soy and quinoa are complete plant proteins that provide all nine essential amino acids from a single source.

What amino acid is the start codon?

AUG codes for methionine — every protein begins with methionine at the N-terminus though it is often removed by post-translational processing in the final mature protein.

What is the difference between essential and non-essential amino acids?

Essential amino acids cannot be synthesised by the human body in sufficient quantities and must come from food. Non-essential amino acids can be made by the body from other metabolic intermediates such as glucose and other amino acids.

What is the smallest amino acid?

Glycine is the smallest amino acid — its side chain is just a single hydrogen atom giving it no chirality and maximum flexibility in protein chains. This unique property makes glycine essential in tight structural positions such as every third residue in collagen.

What amino acids are in collagen?

Collagen is unusually rich in glycine (every third residue), proline, and hydroxyproline. Glycine's small size allows it to fit in the tight core of the collagen triple helix structure, while proline and hydroxyproline provide the rigidity and stability of the helix.

What is the role of cysteine in protein structure?

Cysteine contains a sulphur-containing thiol group that can form disulphide bonds with other cysteine residues. These covalent cross-links stabilise protein tertiary structure and are critical in antibodies, insulin, and many extracellular proteins where structural rigidity is required.