Amino Acids

These are bi-functional compounds. The

contain 2 functions groups:

A primary amine (in most cases) NH2
The carboxylic acid group COOH
The amine and acid groups are both attached to

the same carbon which is called Carbon

Amino Acids are the building blocks of

proteins

AMINO ACIDS STRUCTURE

Non-ionized form

H
Amino
group

H2 N

C
R
Side chain

O
C

Carboxyl
group

OH

Amino Acids
The simplest amino acid is glycine.

H
H

H
N C
H

O
C
O H

Amino Acids
:You must know

O
H2N

CH

Their names
Their structure
Their three letter code
Their one letter code
OH

CH2

Tyrosine, Tyr, Y, aromatic,

hydroxyl
OH

Classification of
of Amino
Amino Acids
Acids
Classification
:There are three main physical categories to describe amino acids
Nonpolarhydrophobicnineinall( 1
Glycine,Alanine,Valine,Leucine,Isoleucine,Methionine,Proline,Phenylalanine
andTryptophan
Unchargedpolar,sixinall( 2
Serine,Threonine,Asparagine,GlutamineTyrosine,Cysteine
Chargedpolar,fiveinall( 3
Lysine,Arginine,Glutamicacid,Asparticacid,andHistidine

Amino 20
Acids
: Note
Variable
R Group

Physical Properties
White solids
The strong attractions in the crystal cause

the high melting point (ex. glycine has a

melting point of 235C)
Normally readily soluble in water
Almost totally insoluble in non-polar
solvents
High dipole moment compare to other
usual acids or bases
Chiral

Chirality
With the exception of glycine, all protein-derived amino
acids have at least one stereocenter and are therefore chiral

CO2
H

NH3
CH3

D-alanine

CO2
H3N

H
CH3

L-alanine

The vast majority of amino acids in the biological world

are the L series

8-26

CHEMICAL
PROPERTIES

1. Amino acids are

Ampholytes
They can act as either an acid or a base
They are Zwitterions or molecules that have
both a positive and a negative charge

Acid-Base Properties of Amino Acids

The ionic forms of the amino acids, shown without

.consideration of any ionizations on the side chain

Acid Base Properties

They are very largely ionic compounds.
The carboxyl group can lose a proton
The amine group can gain a proton
The result is a ZWITTERION.

2. Zwitterions

In aqueous solution depending on the pH,

they form either the neutral form, or the

carboxylate will lose a proton, or the amino
group will gain a proton.

3. Isoelectric Point
For each amino acid there is a definite pH the

isoelectric point at which the acid and basic

ionisations are equal.
The molecule is effectively neutral it carries
equal and opposite charges
This is rarely near pH 7 because the molecule
ionisation tendencies are affected by the other
groups in the molecule
Each amino acid has isoelectric pH (PI) and its
charge will be natural at this pH
By increasing H ions (decreasing pH) it will be
positively charged and visa versa by increasing OH
ions (increasing pH) it will be negatively charged
.

5. Amino acids can form peptide

bonds
Amino acid residue
peptide units
dipeptides

Proteins are
molecules that
consist of one or
more polypeptide
chains

tripeptides
oligopeptides
polypeptides

Peptides are linear polymers that range from 8 to

4000 amino acid residues

Peptide bond formation

one amino acid molecule can react with

another and become joined through an

amide linkage.
This polymerization of amino acids is what
creates proteins.
This condensation reaction yields the newly
formed peptide bond and a molecule of
water.
N-terminal amino acid is on the left side of
the peptide, while C-terminal amino acid is
on the right side

Peptide bond formation

PEPTIDE BOND FORMATION

Glisin + Ala

Gly-Ala
Alanin + Glisin
Ala-Gly
Gambarkan struktur dipeptida !

PEPTIDASE ENZYME
Tripsin : hanya memutus ujung C
Pepsin dan kimotripsin : memutus ujung C dari

Tyr, Phe, Trp

Karboksipeptidase : memutus semua sisi
karboksil
Termolisin : Memutus ujung C dari Ile, Leu, Val
Example :
His-Gly-Tyr-Phe-Arg-Lys-Trp-Asp-Met-Arg-Ala-GlyLys
Reacted with : a. Tripsin
b. Kimotripsin

4. Detecting Amino Acids

EX. (1)
NINHYDRIN TEST

OH

2
O

+ NH2-CH-COOH
OH
CH3

CHO
+ CO2 +
CH3

Note: The product from Pro is

.Yellow and absorbs at 440 nm

N
O

Ruhemanns Purple
nm 570

Ex (2). Millon Reaction

Principle: Millon's reagent (Hg/HNO3) gives positive

results ( pink to dark-red color) with proteins

containing the phenolic amino acid tyrosine
Purpose: To detecte the amino acid that have

phenol group of tyrosin.

Note: some proteins containing tyrosine will initially
form a white precipitate that turns red when heated,
while others form a red solution immediately. Note
that any compound with a phenol group will yield a
positive test, so one should be certain that the
sample being tested does not contain any phenols
other than those present in tyrosine.

Procedure:
1.
2.
3.

In test tube add 2 ml of protein into separate

labeled test tubes.
Add 3-4 drops of Millons reagent, and immerse
the tubes in a boiling water bath for 5 minutes.
Cool the tubes and record the colors formed.

Ex (2). Xanthoprotic Reaction

Some amino acids contain aromatic groups

that are derivatives of benzene.

These aromatic groups can undergo reactions that
are characteristic of benzene and its derivatives.
One such reaction is the nitration of a benzene
ring with nitric acid.
The amino acids tyrosine and tryptophan contain
activated benzene rings and readily undergo
nitration.
The amino acid phenylalanine also contains a
benzene ring, but the ring is not activated and
therefore does not undergo readily nitration.

Principle: Nitric acid gives color when

heated with proteins containing tyrosine

(yellow color) or tryptophan (orange
color); the color is due to nitration.

Purpose: used to identify the presence

of an activated benzene ring.

Note: If one spills a concentrated solution
of nitric acid onto someones skin. The
proteins in skin contain tyrosine and
tryptophan, which become nitrated and
turn yellow.

Procedure
1.

Add 2 ml of protein solution in

a test tube and add 2 drops of
concentrated nitric acid.

2.

The formed white precipitate,

will turn yellow upon heating,
and finally will dissolve giving
a yellow color to the solution.

3.

Cool the solution down.

Carefully add 3 ml of 6 N
NaOH. Note that the yellow
color turns orange.

Ex (3). Glyoxylic Acid

Reaction
Principle: The indole ring reacts with
(Hopkins-Col test):

glyoxylic acid in the presence of a strong

acid to form a violet cyclic product.

Purpose: The Hopkins-Cole test is

specific for tryptophan, the only amino

acid containing indole group. .

Procedure:
Add 1 ml of protein solution in a test tube,

add 1 ml of Hopkins-Col reagent and mix

well.
Incline the test tube and slowly add 1 ml
of concentrated H2SO4 on the inner wall of
the test tube thus forming a reddish violet ring at the interface of the two
layers.

Result:
A reddish violet ring

is formed at the
junction between the
2 layers with albumin
and casein.
.

ELECTROPHORESIS

Kutub negatif

Kutub positif