Properties of amino acids

• Glycine, alanine, valine, serine, tryptophan, histidine

and proline are sweet in taste; leucine is tasteless;
while isoleucine and arginine are bitter
• Sodium glutamate is a flavouring agent
• Aspartame, an artificial sweetener contains aspartic
acid and phenylalanine
• All amino acids have high melting points > 200ºC
• All amino acids are soluble in water and alcohol; but
insoluble in nonpolar solvents
1
Ampholyte and Iso-electric point

• Amino acids can exist as ampholytes or zwitterions

(German word zwitter = hybrid) in solution,
depending on the pH of the medium

+ COOH + COO COO

H3N C H H3N C H H2N C H
CH3 CH3 CH3

Cation Zwitterion Anion

(low pH) (iso-electric pH) (high pH)

2
 Iso-electric pH
• The pH at which the molecule carries no net charge is
known as iso-electric point or iso electric pH (pI)
• In acidic solution they are cationic in form and in
alkaline solution they behave as anions
• At iso-electric pH the amino acids will carry no net
charge; all the groups are ionized but the charges will
cancel each other
• Therefore at iso-electric point, there is no mobility in
an electrical field
• Solubility and buffering capacity will be minimum
3
• To the solution of amino acids if hydrochloric acid is
added drop by drop, at a particular pH, 50% of the
molecules are in cation form and 50 % in zwitterion form
• This pH is pK1 (with regard to COOH)
• If more HCl is added, more molecules become cationic in
nature and solubility increases
• On the other hand, if we titrate the solution from iso-
electric point with NaOH, molecules acquire the anionic
form
• When 50% of molecules are anions, the pH is called pK4 2
• For mono amino mono
carboxylic amino acids;
pI = pK1 + pK2
2
pI of glycine = 2.34 + 9.60
2
= 5.97
From the graph it is evident
that the buffering action is
maximum in and around
pK1 or at pK2 and minimum
5

at pI
• In case of amino acids
having more than two
ionizable groups, Net charge= +1 Net charge= 0 Net charge= -1 Net charge= -2
correspondingly there will
be more pK values
• There are three ionizable
groups and, therefore,
three transitions in the
titration.
• The pI corresponds to the
midpoint between the two
transitions that involve the
species with no net
charge. 6
 pK values of amino acids
Name of the amino pK1 of alpha pK2 of alpha pK3 of extra Extra pI
acid carboxyl amino group ionizable ionizable
gorup group group present

Glycine 2.3 9.6 5.9

Valine 2.3 9.6 6.0
Serine 2.2 9.2 5.7
Cysteine 1.9 10.3 8.2 Sulfhydryl 5.1
Glutamine 2.2 9.1 5.6
Aspartic acid 2.1 9.8 3.9 β-carboxyl 3.0
Glutamic acid 2.2 9.6 4.3 γ-carboxyl 3.2
Lysine 2.2 8.9 10.5 ε-amino 9.7
Arginine 2.0 9.0 12.5 Guanidinium 10.8
Phenylalanine 2.6 9.2 5.9
Tyrosine 2.2 9.1 10.1 Phenol 5.7
Tryptophan 2.4 9.4 5.9
Histidine 1.8 9.2 6.1 Imidazole 7.67
 Effective buffer

• The pK value of imidazolium group of Histidine is

6.1 and therefore effective as a buffer at the
physiological pH of 7.4
• The buffering capacity of plasma proteins and
hemoglobin is mainly due to histidine residue

8
 Optical activity
• Amino acids having an asymmetric carbon atom exhibit
optical activity
• Glycine is the simplest amino acid and has no
asymmetric carbon atom and therefore shows no optical
activity
• All others are optically active
• The mirror image forms produced with reference to the
alpha carbon atom, are called D and L isomers
• L-amino acids occur in nature and are therefore called
natural amino acids
10
11
Reactions due to carboxyl group

1. Decarboxylation

2. Amide formation

12
 1. Decarboxylation
• The amino acids will undergo alpha decarboxylation to
form the corresponding amine

COOH

CH – NH2 CH2 – NH2 + CO2

R R

• Some of the important amines produced from amino

acids are
– Histidine Histamine + CO 2
– Tyrosine Tyramine +CO 2
– Tryptophan Tryptamine + CO 2
– Glutamic acid GABA + CO 2
13
– Lysine Cadaverine + CO 2
 2. Amide formation
• The – COOH group of dicarboxylic amino acids can
combine with ammonia to form the corresponding
amide. For example,
– Aspartic acid + NH3 Asparagine
– Glutamic acid + NH3 Glutamine
• These amides are also components of protein
structure
• The amide group of glutamine serves as the source of
nitrogen for nucleic acid synthesis
14
 Reactions due to amino group

1. Transamination

2. Oxidative deamination

3. Formation of carbamino compound

15
 1. Transamination
COO COO
• The alpha amino group
COO CH2 COO CH2
of amino acid can be
CH2 CH2 CH2 CH2
transferred to alpha
HC N H 3+ + C O C O + HC N H 3+
ketoacid to form the COO COO COO COO
corresponding new a s p a r ta te  -k e to g lu ta r a te o x a lo a c e ta te g lu ta m a te
amino acid and alpha A m in o tr a n s f e r a s e ( T r a n s a m in a s e )
ketoacid COO COO
• This is an important CH2 CH2

reaction in the body for CH3 CH2 CH3 CH2

the interconversion of HC N H 3+ + C O C O + HC N H 3+

amino acids and for COO COO COO COO

synthesis of non- a la n in e  -k e to g lu ta r a te p y r u v a te g lu ta m a te
A m in o tra n s fe ra s e (T ra n s a m in a s e )
essential amino acids 16
 2. Oxidative deamination
• The alpha amino group
is removed from the N H 3+
amino acid to form the 
H2 H2
OOC C C C COO
corresponding ketoacid
glutam ate
and ammonia H
N A D (P ) +
H 2O
• In the body, glutamic N AD(P)H
acid is the most O
H2 H2
common amino acid to 
OOC C C C C O O  + N H 4+
undergo oxidative  -ketoglutarate
deamination G lutam ate D ehydrogenase

17
3. Formation of carbamino compound

• Carbon dioxide adds to the alpha amino group of

amino acids to form carbamino compounds
• The reaction occurs at alkaline pH and serves as a
mechanism for the transport of carbon dioxide from
tissues to the lungs by hemoglobin

Hb – NH2 +CO2 Hb – NH – COOH

(carbamino – Hb)

18
 Reactions due to side chains

1. Transmethylation

2. Ester formation by the OH group

3. Reactions of the amide group

4. Reactions of SH group

19
 1. Transmethylation
• The methyl group of methionine, after activation,
may be transferred to an acceptor which becomes
methylated

20
 2. Ester formation by the OH group
• The hydroxy amino acids
can form esters with
phosphoric acid
• In this manner the serine
and threonine residues of
proteins are involved in the
formation of
phosphoproteins

Similarly these hydroxyl groups can form O-glycosidic bonds

with carbohydrate residues to form glycoproteins 21
 3. Reaction of amide group

• The amide groups of glutamine and asparagine can

form N-glycosidic bonds with carbohydrate residues
to form glycoproteins

22
 4. Reactions of SH group
• Cysteine has a sulfhydryl
(SH) group and it can form a
disulphide (S-S) bond with
another cysteine residue
• The two cysteine residues
can connect two polypeptide
chains by the formation of
interchain disulphide bonds
• The dimer formed by two
cysteine residues is
sometimes called cystine or
dicysteine 23
 Amino acid derivatives of importance
• Gamma aminobutyric acid (GABA, a derivative of
glutamic acid) and dopamine (derived from tyrosine) are
neurotransmitters .
• Histamine (synthesized from histidine) is the mediator of
allergic reactions.
• Thyroxine (from tyrosine) is an important thyroid
hormone.
• Cycloserine, a derivative of serine is an antituberculous
drug.
• Histidine residues are important in the buffering activity
of proteins.
• Ornithine and citrulline are derivatives of arginine, and
are essential for urea synthesis. 24
 Peptide bond formation
• Alpha carboxyl group of
one amino acid reacts
with alpha amino group
of another amino acid to
form a peptide bond or
CO-NH bridge
• Proteins are made by
polymerization of amino
acids through peptide
bonds

25
 Color reactions of aminoacids

Reaction Answered by specific group

1.) Biuret reaction Peptide bonds

2.) Ninhydrin Alpha amino group

3.) Xanthoproteic test Benzene ring (Phe,Tyr,Trp)

4.) Millon’s test Phenol(Tyrosine)

5.) Aldehyde test Indole(Tryptophan)

6.) Sakaguchi’s test Guanidinium(Arginine)

7.) Sulfur test Sulfhydryl(Cysteine)

8.) Nitroprusside test Sulfhydryl(Cysteine)

9.) Pauly’s test Imidazole(Histidine)

26
 Proteins
• The word protein is derived from Greek word,
“proteios” which means primary
• Out of the total dry body weight, 3/4ths are made up of
proteins
• Proteins are used for the body building; all the major
structural and functional aspects of the body are
carried out by protein molecules
• Abnormalities in protein structure will lead to
molecular diseases with profound alterations in
metabolic functions
27
 Proteins
• Proteins contain Carbon, Hydrogen, Oxygen and
Nitrogen as the major components while Sulphur and
Phosphorous are minor constituents
• Nitrogen is characteristic of proteins
• On an average, the nitrogen content of ordinary
proteins is 16% by weight
• All proteins are polymers of amino acids

28
 Peptide bond formation
• Alpha carboxyl group of
one amino acid reacts
with alpha amino group
of another amino acid to
form a peptide bond or
CO-NH bridge
• Proteins are made by
polymerization of amino
acids through peptide
bonds

29
 Amino acids are linked by peptide
bonds
• Dipeptide: 2 amino acids (aas) joined by 1 peptide
bond.
• Tripeptide: 3 aas joined by 2 peptide bonds.
• Tetrapeptide: 4 aas joined together by 3 peptide
bonds.
• Pentapeptide and so forth….
• Oligopeptide: Few aas joined together by peptide
bonds.
• Polypeptide: 10-50 aas joined. Molecular weights
generally below 10000.
• Proteins: More than 50 aas joined. Generally have
high molecular weights.
30
 Structure of proteins
• Proteins have different levels of structural organization;
primary, secondary, tertiary and quaternary

31
 Levels of organisation

• Definitions
• Primary structure:- means the order of amino acids in the
polypeptide chain and the location of disulfide bonds, if
any.
• Secondary structure:- is the steric relationship of amino
acids, close to each other.
• Tertiary structure:-denotes the overall arrangement and
inter relationship of the various regions,or domains of a
single polypeptide chain.
• Quaternary structure:- results when the proteins consist of
two or more polypeptide chains held together by non
covalent forces.
32
Levels of organisation of proteins
• Primary structure:- is
determined by the sequence
of aminoacids.
• Secondary structure:- occurs
when the amino acids are
linked by hydrogen bonds.
• Tertiary structure:- is formed
when alpha helices and beta
sheets are held together by
weak interactions.
• Quaternary structure:-
consists of more than one
polypeptide chain.
33