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Amino Acids
“When you understand the amino acids,
you understand everything”
©CMBI 2001
Amino Acids
Proteins are macromolecules made up from 20 different amino acids.
The heart of the amino acid is the so-called C. To which are bound: an
amino group, a carboxyl group, a hydrogen, and the side chain.
O
H2N
C
CH

OH
R
The C, C, N and O atoms are called backbone atoms.
R denotes any one of the 20 possible side chains.
©CMBI 2001
Di-peptide
Amino acids bind, to form a protein.
Upon binding, two protons from the
NH3 and one oxygen from the
carboxyl join to form a water. So the
peptide bond has at the one side a
C=O and at the other side an N-H.
Only the ends of the chain are NH3 or
carboxylic, and thus charged.
Which dipeptide is this?
Where are the charges?
©CMBI 2001
Phi-Psi
©CMBI 2001
Amino Acid Sequence
The amino acid sequence (also called primary structure) of a
protein is the order of the amino acids in the protein chain.
The sequence is always read from the N-terminus to the Cterminus of the protein.
For example:
+H3N-Lys-Val-Phe-Ala-Met-Cys-Leu-Leu-Arg-Val-COO-
Or (in one-lettercode):
KVFAMCLLRV
©CMBI 2001
The 20 Amino Acids
A
C
D
E
F
G
H
I
K
L
M
N
P
Q
R
S
T
V
W
Y
Ala
Cys
Asp
Glu
Phe
Gly
His
Ile
Lys
Leu
Met
Asn
Pro
Gln
Arg
Ser
Thr
Val
Trp
Tyr
Alanine
Cysteine
Aspartic acid (Aspartate)
Glutamic acid (Glutamate)
Phenylalanine
Glycine
Histidine
Isoleucine
Lysine
Leucine
Methionine
Asparagine
Proline
Glutamine
Arginine
Serine
Threonine
Valine
Tryptophan
Tyrosine
©CMBI 2001
20 Amino Acids
The side chains, R, determine the differences in the structural and
chemical properties of the 20 ‘natural’ amino acids.
The 20 amino acids can, for example, be classified as follows:
Aliphatic/hydrophobic
Polar
Alcoholic
Sulfur-containing
Aromatic
Charged
Special
Ala, Leu, Ile, Val
Asn, Gln
Ser, Thr, (Tyr)
Met, Cys
Phe, Tyr, Trp, (His)
Arg, Lys, Asp, Glu, (His)
Gly (no R), Pro (cyclic)
Several amino acids belong in more than one category.
©CMBI 2001
Amino Acid Characteristics
There are many ways to characterize the properties of amino acids.
The ones most useful and most commonly used are:
Hydrophobicity
Size
Charge
Secondary structure preference
Alcoholicity
Aromaticity
And on top of that there are some special characteristics like bridge
forming by cysteines, rigidity of prolines, titrating at physiological
pH of histidine, flexibility of glycines, etc.
©CMBI 2001