1 letter code	3 letter code	amino acid	size	Hydrophylic Hydrophobic Inbetween (I)	charge	sec. structure preference	special properties	2D image	3D image
A	Ala	Alanine	L M S	Phylic Phobic I	+ 0 -	H S T None	occurs relatively often good for mutation (Ala-scan) aliphatic (only CH3 as side chain)
C	Cys	Cysteine	L M S	Phylic Phobic I	+ 0 -	H S T None	reactive S-H group allows cys-cys bridges cys-cys bridges stabilizes protein can bind metal ions (esp. Zn, Cu)
D	Asp	Aspartic acid	L M S	Phylic Phobic I	+ 0 -	H S T None	side chain titrates at pH 4.5 can bind ions (mainly Ca) easily forms H-bonds with own/local backbone
E	Glu	Glutamic acid	L M S	Phylic Phobic I	+ 0 -	H S T None	side chain titrates at pH 4.6 only one C larger than Asp (D), but different properties
F	Phe	Phenylalanine	L M S	Phylic Phobic I	+ 0 -	H S T None	aromatic
G	Gly	Glycine	L M S	Phylic Phobic I	+ 0 -	H S T None	no side chain -> flexible backbone smallest residue
H	His	Histidine	L M S	Phylic Phobic I	+ 0 -	H S T None	little aromatic often in active sites can bind metal ions (Zn, Ni, Cu)
I	Ile	Isoleucine	L M S	Phylic Phobic I	+ 0 -	H S T None	helix ok dislikes turn
K	Lys	Lysine	L M S	Phylic Phobic I	+ 0 -	H S T None	dislikes strand helix & turn ok long and flexible side chain
L	Leu	Leucine	L M S	Phylic Phobic I	+ 0 -	H S T None	dislikes turn
M	Met	Methionine	L M S	Phylic Phobic I	+ 0 -	H S T None	strand ok, dislikes turns can bind metals with sulphur often first residue in molecule N-terminus mostly positive -> surface (forced marriage)
N	Asn	Asparagine	L M S	Phylic Phobic I	+ 0 -	H S T None	dislikes helix, un-amused in strand can bind metal ions (Cu)
P	Pro	Proline	L M S	Phylic Phobic I	+ 0 -	H S T None	side chain twice connected to backbone (at Cα and N)->prebend imino acid unless N-terminal, not good for helices and strands (no backbone proton) despite hydrophobicity often at surface (likes turns, disrupts secondary structure)
Q	Gln	Glutamine	L M S	Phylic Phobic I	+ 0 -	H S T None	not picky about secondary structure isosteric with glutamic acid
R	Arg	Arginine	L M S	Phylic Phobic I	+ 0 -	H S T None	not picky about secondary structure side chains contain rigid guadinium group
S	Ser	Serine	L M S	Phylic Phobic I	+ 0 -	H S T None	side chain is an alcohol often active site in enzyme with H & D
T	Thr	Threonine	L M S	Phylic Phobic I	+ 0 -	H S T None	side chain is an alcohol beta-branched -> likes beta-strands occasionally in metal binding (Ca)
V	Val	Valine	L M S	Phylic Phobic I	+ 0 -	H S T None	beta-branched -> likes beta-strands isosteric with threonine dislikes turns, helices ok
W	Trp	Tryptophan	L M S	Phylic Phobic I	+ 0 -	H S T None	biggest residue aromatic despite nitrogen (donor for hydrogen bonds) in five-ring, very hydrophobic
Y	Tyr	Tyrosine	L M S	Phylic Phobic I	+ 0 -	H S T None	side chain is alcohol aromatic

Mnemonics

Codes

The properties