1 nm · Molecules
Amino acids
Nonpolar (hydrophobic)
9
Glycine
Gly · G
side chain –H
hydrophobic
pKa 2.34 / 9.60 · pI 5.97
The only achiral amino acid: its α-carbon carries two hydrogens.
Alanine
Ala · A
side chain –CH₃
hydrophobic
pKa 2.34 / 9.69 · pI 6.01
Simplest chiral amino acid; a plain methyl side chain.
Valine
Val · V
side chain –CH(CH₃)₂
hydrophobicessential
pKa 2.32 / 9.62 · pI 5.97
Branched-chain amino acid (BCAA). Glu→Val at position 6 of β-globin causes sickle cell disease.
Leucine
Leu · L
side chain –CH₂CH(CH₃)₂
hydrophobicessential
pKa 2.36 / 9.60 · pI 5.98
BCAA, and one of only two purely ketogenic amino acids.
Isoleucine
Ile · I
side chain –CH(CH₃)CH₂CH₃
hydrophobicessential
pKa 2.36 / 9.68 · pI 6.02
BCAA with two chiral centers (the α- and β-carbons). Both glucogenic and ketogenic.
Methionine
Met · M
side chain –CH₂CH₂SCH₃
hydrophobicessential
pKa 2.28 / 9.21 · pI 5.74
Start codon AUG. Its sulfur is a thioether, so it cannot form disulfide bonds.
Proline
Pro · P
side chain cyclic –CH₂CH₂CH₂– back to N
hydrophobic
pKa 1.99 / 10.96 · pI 6.48
Secondary amine (an imino acid). Its rigid ring kinks α-helices and breaks secondary structure.
Phenylalanine
Phe · F
side chain –CH₂–C₆H₅
hydrophobicessential
pKa 1.83 / 9.13 · pI 5.48
Aromatic, purely nonpolar benzyl group. Accumulates in PKU.
Tryptophan
Trp · W
side chain –CH₂–indole
hydrophobicessential
pKa 2.38 / 9.39 · pI 5.89
Bulkiest side chain, an indole ring. Dominates absorbance at 280 nm. Precursor to serotonin and niacin.
Polar, uncharged
6
Serine
Ser · S
side chain –CH₂OH
polar
pKa 2.21 / 9.15 · pI 5.68
Hydroxyl side chain: a phosphorylation site and a catalytic-triad nucleophile.
Threonine
Thr · T
side chain –CH(OH)CH₃
polaressential
pKa 2.11 / 9.62 · pI 5.87
Hydroxyl and methyl; with isoleucine, one of the two amino acids with two chiral centers.
Cysteine
Cys · C
side chain –CH₂SH
polar
pKa 1.96 / 10.28 / R 8.18 · pI 5.07
A thiol. Two cysteines oxidize to a disulfide bond, forming cystine. The only chiral amino acid with (R) configuration.
Tyrosine
Tyr · Y
side chain –CH₂–C₆H₄–OH
polar
pKa 2.20 / 9.11 / R 10.07 · pI 5.66
Aromatic and polar (a phenol OH). Precursor to thyroid hormone, dopamine and melanin.
Asparagine
Asn · N
side chain –CH₂CONH₂
polar
pKa 2.02 / 8.80 · pI 5.41
The amide of aspartate: uncharged, not acidic. Site of N-linked glycosylation.
Glutamine
Gln · Q
side chain –CH₂CH₂CONH₂
polar
pKa 2.17 / 9.13 · pI 5.65
The amide of glutamate. The main carrier of ammonia in blood, to the liver and kidneys.
Acidic (−)
2
Aspartic acid
Asp · D
side chain –CH₂COO⁻
acidic
pKa 1.88 / 9.60 / R 3.65 · pI 2.77
Negatively charged at pH 7. Donates the second nitrogen of urea in the urea cycle.
Glutamic acid
Glu · E
side chain –CH₂CH₂COO⁻
acidic
pKa 2.19 / 9.67 / R 4.25 · pI 3.22
Negatively charged at pH 7. Main excitatory neurotransmitter; hub of transamination.
Basic (+)
3
Lysine
Lys · K
side chain –(CH₂)₄NH₃⁺
basicessential
pKa 2.18 / 8.95 / R 10.53 · pI 9.74
Long, flexible, positively charged amine. Site of histone acetylation. Purely ketogenic.
Arginine
Arg · R
side chain –(CH₂)₃NH–C(=NH₂⁺)NH₂
basic
pKa 2.17 / 9.04 / R 12.48 · pI 10.76
A guanidinium group: the most basic side chain (pKₐ ≈ 12.5), positive at every physiological pH. Conditionally essential: made in the urea cycle, but needed from the diet during growth.
Histidine
His · H
side chain –CH₂–imidazole
basicessential
pKa 1.82 / 9.17 / R 6.00 · pI 7.59
An imidazole, pKₐ ≈ 6: the only side chain that buffers near physiological pH. Coordinates heme iron.
Bonds and links
Peptide bond
Formed by dehydration; broken by hydrolysis. Rigid and planar thanks to resonance.
Cystine (disulfide)
Two cysteines oxidized together. β-mercaptoethanol reduces it back.