You are on page 1of 77

Department of Chemistry /

Biochemistry / Molecular
What are amino acids ?
Structure of Amino acids
Classification of Amino acids
Reactions of amino acids (chemistry e.t.c.)
Proteins functions and amino acid derivatives.
Methods of isolation and identification
Proteins mediate virtually every process that takes place in a
cell, exhibiting an almost endless diversity of functions.
Proteins are the most abundant biological macromolecules,
occurring in all cells and all parts of cells.
Proteins are the molecular instruments through which
genetic information is expressed.
All proteins, whether from the most ancient lines of
bacteria or from the most complex forms of life, are
constructed from the same ubiquitous set of 20 amino acids,
covalently linked in characteristic linear sequences.
Proteins are found in a wide range of sizes, from relatively
small peptides with just a few amino acid residues to huge
polymers with molecular weights in the millions.
What is most remarkable is that cells can produce proteins
with strikingly different properties and activities by joining the
same 20 amino acids in many different combinations and
sequences. Fromthese building blocks different organisms can
make such widely diverse products as enzymes, hormones,
antibodies, transporters, muscle fibers, the lens protein of the
eye, feathers, spider webs, rhinoceros horn, milk proteins,
antibiotics, mushroom poisons, and myriad other substances
having distinct biological activities
They are the building blocks of proteins.
They are organic compounds, which contain two
functional groups, amino group (-NH2) and carboxyl
group (-COOH).
The amino group is usually attached to the -carbon
atom (next to the -COOH group).
Amino acids present in proteins are of the -L-type i.e.
the amino (H2N-) group is present on the left side of the
vertical formula.
Hydrogen for R,
most simple,
Methyl for R, a
simple functional
group to start just
like A (in alanine)
starts the alphabet
Valine (V)
simple again,
but shaped
like the V in
its name
extended by
Proline (P) 3
carbon chain to
prolines own
special and
found in turns
(Met) (M)
special - starts every
protein, 3 carbons
with a thioether;
sulfhydryl alanine,
reactive, can form
alanine with a phenol
group which you
KNOW is aromatic, the
Y in phenyl can
remind you which 3
amino acids with names
beginning with T (the
Ts) are aromatics
one of 3 Ts
that has Y in its
name so it is an
one of 3 Ts with a Y so it is aromatic, will
tryp you up because it is hard to
has a 3 carbon start to N (or indole ring on
one of 3 Ts, without
Y so aliphatic (also
its symbol is the first
letter of its name like
the other aliphatics), its
threo parts are
methyl, hydroxyl, and
hydrogen on a single C
carboxyl alanine
with acidic nature
by suffix ate, the
alphabetical ordering
the first letter of their
names correlates with
an increase in length
of side chain
plus one
methylene, G
is after A
3 carbon chain
linked to a C full of
only Ns
(no Hs & C has 4
bonds) through an
3 carbon chain
plus one
methylene to
it lies (Lys)
about the 3
carbon trend
(His) (H)
3 carbons to N and
loop back through C
n N
of aspartate
derivative of
Amino acids can be classified in 4 ways:
1. Based on structure
2. Based on the side chain characters
3. Based on nutritional requirements
4. Based on metabolic fate
30 Biochemistry For Medics
They are classified in three broad categories:
Mono amino mono carboxylic acid
It is further subdivided in 5 groups:
a. Simple amino acids-example: glycine, alanine
b. Branched chain amino acids-eg: valine,leucine,isoleucine
c. Hydroxyl group containing amino acids-eg: serine, threonine
d. Sulphur containing amino acids-eg: cysteine, cystine,
e. Amide group containing amino acids-e.g.- asparagine,
1)Classification based on structure
Mono amino dicarboxylic acid
Example :aspartic acid, glutamic acid
Di /poly amino mono carboxylic acid
Example : lysine, arginine
1)Classification based on structure
1)Classification based on structure
I. Aliphatic Amino Acids:
a) Mono-amino mono-carboxylic acids:
Simple amino acids: Glycine , Alanine
1)Classification based on structure
I. Aliphatic Amino Acids:
a) Mono-amino mono-carboxylic acids:
Branched chain amino acids: Valine, Leucine and Isoleucine
1)Classification based on structure
I. Aliphatic Amino Acids:
a) Mono-amino mono-carboxylic acids:
-OH group-containing amino acids: Serine and Threonine
1)Classification based on structure
I. Aliphatic Amino Acids:
a) Mono-amino mono-carboxylic acids:
Sulfur-containing amino acids: Cysteine, Cystine(Formed by linking of
two cysteine residues) and Methionine.
1) Classification based on structure
I. Aliphatic Amino Acids:
a) Mono-amino mono-carboxylic acids:
Amide group-containing amino acids:
Glutamine and Asparagine
1) Classification based on structure
I. Aliphatic Amino Acids:
a) Mono-amino di-carboxylic acids: Aspartic acid and
Glutamic acid
1) Classification based on structure
I. Aliphatic Amino Acids:
a) Di- basic mono-carboxylic acids:
Arginine and Lysine
1) Classification based on structure
ii ) Aromatic amino acids-
Phenyl alanine and tyrosine
1)Classification based on structure
iii) Heterocyclic Amino Acids: Tryptophan and Histidine
1)Classification based on structure
iv) Imino acid- Proline
Hydroxl proline
1)Classification based on structure
V.Derived Amino Acids:
Non--amino acids
e.g.: -alanine, -amino butyric acid
(GABA), -amino Levulinic acid
1) Classification based on structure
V.Derived Amino Acids:
Derived and Incorporated in tissue
e.g.: Hydroxy-proline, hydroxy-lysine
1) Classification based on structure
V. Derived Amino Acids:
Derived but not incorporated in tissue proteins:
e.g.: Ornithine, Citrulline, Homocysteine, Argino
succinic acid
2) Classification based on side chain characters
A. Amino acids with a non-polar side-chain:
e.g.: Alanine, Valine, Leucine, Isoleucine, Phenylalanine,
Tryptophan, Proline
Each of these amino acids has a side chain that does not
bind or give off protons or participates in hydrogen or ionic
Side chains of these amino acids can be thought of as
Oily or lipid like, a property that promotes hydrophobic
Amino acids with a non-polar side-chain:
2) Classification based on side chain characters
B) Amino acids with a polar but uncharged side-chain:
e.g. Serine, Threonine, Tyrosine, Cysteine, Asparagine and
These amino acids are uncharged at neutral pH,
although the side chains of cysteine and Tyrosine
can lose a proton at an alkaline pH.
Serine , Threonine and Tyrosine each contains a polar hydroxyl group
that can participate in hydrogen bond formation.
Side chains of Asparagine and Glutamine
contain a carbonyl group and amide group, they can also participate in
hydrogen bond formation.
Amino acids with a polar but uncharged
2) Classification based on side chain characters
C) Amino acids with a charged side-chain
a)Amino acids with a positively charged side-chain:
The basic amino acids- Lysine, Arginine and
b)Amino acids with a negatively charged side-chain:
The acidic amino acids- Glutamic acid and Aspartic
They are hydrophilic in nature.
Amino acids with a charged side-chain
3)- Classification based on nutritional requirements
I. Essential amino acids:
These amino acids cannot be synthesized in the body and have to be
present essentially in the diet. Examples-Valine, Isoleucine, Leucine,
Lysine, Methionine, Threonine, Tryptophan and Phenylalanine.
II. Semi-essential amino acids:
These amino acids can be synthesized in the body but the rate of
synthesis is lesser than the requirement(e.g. during growth, repair
or pregnancy) Examples-Arginine and Histidine.
III. Non-essential amino acids:
These amino acids are synthesized in the body, thus their absence in
the diet does not adversely affect the growth.
Examples- Glycine, Alanine, and the other remaining amino acids.
4)-Classification based on metabolic fate
The carbon skeleton of amino acids can be used either for glucose
production or for the production of ketone bodies, Based on that
I. Both glucogenic and ketogenic amino acids:
Isoleucine, Tyrosine, Phenylalanine and Tryptophan
II. Purely Ketogenic amino acids:
Leucine and Lysine
III. Purely Glucogenic amino acids:
The remaining 14 amino acids are glucogenic. Alanine, valine
,serine, threonine, glycine, methionine, asparagine,
glutamine, cysteine, cystine, aspartic acid, glutamic acid,
histidine and arginine.
Of the over 300 naturally occurring amino
acids, 20 constitute the monomer units of
proteins. These 20 amino acids are called the
Primary or Standard amino acids.
Seleno cysteine is the 21
Amino Acid
The other are Pyroglutamate and Pyrolysine.
Each amino acid has three letter (code) and one
letter (Symbol) abbreviations-
Examples-1) Unique first letter
Cysteine- Cys- C
Histidine- His- H
2) Priority of commonly occurring amino acids
Alanine- Ala- A (Preference over Aspartate)
Glycine- Gly-G (Preference over Glutamate)
3) Similar sounding names- Some one letter
symbols sound like the amino acids they
represent- Example
Tryptophan W (Twyptophan)
Phenyl alanine F
4) Letters close to initial letter
Aspartate- Asx- B( near A)
Lysine Lys- K(near L)
Amino acid abbreviations
Arginine - Guanidiniumgroup
Phenyl Alanine- Benzene group
Tyrosine - Phenol group
Tryptophan - Indole group
Histidine - Imidazole group
Proline - Pyrrolidine
Proline has a secondary amino group, hence it
is an imino acid.
Properties of amino acids
Physical properties-
May be sweet(Glycine, Alanine, Valine),
tasteless(Leucine) or bitter(Arginine, Isoleucine).
Aspartame- An artificial sweetener contains Aspartic
acid and Phenyl alanine.
Soluble in water, acids, alkalis but insoluble in organic
High melting point(More than 200
Amino acids can exist as ampholytes or zwitterions in
solution, depending upon pH of the medium.
The pH at which the amino acids exist as zwitterions,
with no net charge on them is called Isoelectric pH or
Isoelectric point.
In acidic medium, the amino acids exist as cations
In alkaline medium , they exist as anions.
If HCl is added drop wise to am amino acid solution, at
a particular pH, 50 % of the molecules are in the cationic
form and 50% are in the zwitterion form. This pH is pK1
(with regard to COOH)
If the titration is done from the Isoelectric point with
NaOH, molecules acquire the anionic form. When 50 % of
the molecules are in the anionic form and 50% are in the
zwitterion form. This pH is pK2(with regard to NH
For mono amino mono
carboxylic amino acids-
pI = pK1+pK2
The buffering action is
maximum in and around
pK1 or at pK2 but is
minimum at pI
of some amino acids
The carbon of each amino acid is attached to four different
groups and is thus a chiral or optically active carbon atom.
Glycine is exceptional because there are two hydrogen
substituents at the carbon, thus it is optically inactive.
Amino acids with asymmetric centre at the carbon can
exist in two forms, D and L forms that are mirror images of
each other and are called Enantiomers.
All amino acids found in proteins are of L- configuration
D- amino acids are found in some antibiotics and in bacterial
cell walls.
7/5/2012 Biochemistry For Medics 66
L & D isomers of amino acids
1) Reactions due to amino group
2) Reactions due to carboxyl group
3) Reactions due to side chain
4) Reaction due to both amino and carboxyl
Reactions due to amino group
Oxidative deamination- amino group is removed and
corresponding -keto acid is formed. -keto acid
produced is either converted to glucose or ketone
bodies or is completely oxidized.
Transamination-Transfer of an amino group from
an amino acid to an keto acid to form a new amino
acid and a corresponding keto acid.
Reactions due to amino group
Formation of carbamino compound
CO2 binds to amino acid on the globin chain of
hemoglobin to form carbamino hemoglobin
The reaction takes place at alkaline pH and serves as
a mechanism for the transfer of Carbon dioxide from
the tissues to the lungs by hemoglobin.
1) Decarboxylation- Amino acids undergo alpha decarboxylation to
form corresponding amines. Examples-
Glutamic acid GABA
Histidine Histamine
Tyrosine Tyramine
2) Formation of amide linkage
Non carboxyl group of an acidic amino acid reacts with ammonia
by condensation reaction to form corresponding amides
Aspartic acid Asparagine
Glutamic acid Glutamine
Reactions due to side chains
1) Ester formation
OH containing amino acids e.g. serine, threonine
can form esters with phosphoric acid in the
formation of phosphoproteins.
OH group containing amino acid can also form:
Glycosides by forming
O- glycosidic bond with carbohydrate residues.
2) Reactions due to SH group (Formation of disulphide
Cysteine has a sulfhydryl group( SH) group and can
form a disulphide (S-S) bond with another cysteine
The dimer is called Cystine
Two cysteine residues can connect two polypeptide
chains by the formation of interchain disulphide chains.
Reactions due to side chains
The methyl group of Methionine can be
transferred after activation to an acceptor for the
formation of important biological compounds.
4)Reactions due to both amino & carboxyl groups
Formation of peptide bond
Reactions due to side chains
Incorporated in to tissue proteins
Niacin, Serotonin and melatonin are synthesized from
Melanin, thyroid hormone, catecholamines are
synthesized from Tyrosine
GABA (neurotransmitter) is synthesized from Glutamic
Nitric oxide, a smooth muscle relaxant is synthesized
from Arginine.
Act as precursors for haem, creatine and glutathione,
Porphyrins, purines and pyrimidines.
S.No. Test Significance
1) Ninhydrin reaction Given by all Alpha amino acids
2) Xanthoproteic test Given by aromatic amino acids
3) Millons test Confirmatory test for Tyrosine
4) Biuret test Not given by free amino acids
5) Sakaguchi test Given by Arginine
6) Hopkins Cole reaction Confirmatory test for Tryptophan
7) Lead acetate test Given by cysteine and cystine but
not given by Methionine
8) Nitroprusside reaction Given by SH group containing