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Amino Acids
The compounds containing amino group (-NH2) and carboxylic group (-
COOH) are called amino acids. The general structure is:
All amino acids contain a carbon atom in the middle of the molecule,
the alpha-carbon
This atom is surrounded by three chemical groups.
One is an amine group -NH2
The second one is a carboxyl group -OOOH
The third group is denoted by R. This is the variable radical group
and is different for every amino acid. This R group makes the amino
acid unique.
i. Glycine (H)
ii. Alanine (CH3)
iii. Valine ( CH (CH3)2 )
iv. Methionine ( CH2CH2SCH3 )
v. Leucine ( CH2CH(CH3)2 )
vi. Isoleucine ( -CH(CH3)CH2CH3 )
vii. Proline (special structure)
viii. Phenylalanine
ix. Tryptophan
If the side chains of amino acid contain different polar groups like
amines, alcohols or acids they are polar in nature. These are also known
as Hydrophilic Acids. These are further divided into three further
categories.
i. Histidine
ii. Lysine ( CH2(CH2)2NH2 )
iii. Arginine
c) Neutral: These are neither acidic nor basic. They have an equal
number of amino and carboxyl groups. Also, they have at least one
hydrogen component connected to electronegative atoms. Some of these
neutral acids are
i. Serine ( CH2OH )
ii. Threonine ( CH(OH)CH3 )
iii. Asparagine ( CH2OHNH2 )
iv. Glutamine ( CH2CH2CONH2 )
v. Cysteine ( CH2SH )
vi. Tyrosine
Amino acid can also be classified on the basis of their need to the
human body and their availability in the human body
Now that we have seen the structure and types of amino acids.
Now from this information, we can arrive at the properties of amino
acids.
Each amino acid has both an acidic and basic group as you can see
from its structure. This is the reason they behave like salts.
Any amino acid in the dry state is in crystalline form. They exist as a
dipolar ion. The COOH group exists as an anion. And the NH2 group
exists as a cation. This dipolar ion has a special name “Zwitter ions’.
In aqueous solution, alpha amino acids exist in equilibrium between
a cationic form, an anionic form and dipolar ion.
The Isoelectric point is the pH point at which the concentration of
zwitter ions is the highest ad the concentration of cationic and
anionic form is equal. This point is definite for every α-amino acid.
They are generally water soluble and also have high melting points.
Leucine
Isoleucine
Lysine
Theorine
Methionine
Phenylalanine
Valine
Tryptophan
Histidine (conditionally essential)
Non-Essential Amino Acids
These acids are synthesized in our bodies itself and we need not
rely on outside sources for them. They are either produced in our bodies
or obtained from protein breakdowns.
Zwitter ion
1. Amino acid contains both basic acidic (carboxyl group) and basic
(amino group) groups in the same molecule. In aque-ous solution, the
carboxyl group loses a proton which is accepted by the NH2 group
which results in the formation of a dipolar ion known as Zwitter ion.
This is neutral but contains both positive and negative charges.
Isoelectric point
The pH at which this dipolar ion stops moving towards the respective
electrode is known as isoelectric point. At isoelectric point, the amino acids
have the least solubility in water.
Peptides
Peptides are condensation products of two or more amino acid
Dipeptide has only one peptide bond, tripeptide has two peptide bonds and so
on. Thus, a polypeptide made up of n-amino acids has (n – 1) peptide bonds.
Peptide Linkage
For example:
Classification of Peptides:
Polypeptides
Classification of Protein
Fibrous proteins: The polypeptide chains run parallel and are held
together by hydrogen and disulphide bond forming a fibre like
structure
For example: Keratin (present in hair, wool, silk) and myosin (present in
muscles), etc.
Structure of Proteins
There are two kinds of shapes formed in the secondary structure. These
are
This is the structure that gives protein the 3-D shape and
formation. After the amino acids form bonds (secondary structure) and
shapes like helices and sheets, the structure can coil or fold at random.
This is what we call the tertiary structure of proteins. If this structure is
disrupted or disturbed a protein is said to be denatured which means it is
chemically affected and its structure is distorted.
Quaternary Structure
(ii) Conjugated proteins These yield α-amino acids and non-protein part,
called prosthetic group.
Glycoproteins Carbohydrates
Metalioproteins Metals
Lipoproteins Lipids
Two chains containing 141 amino acid residues each are called α-chains and
the two chains containing 146 amino acid residues are called β-chains.
Denaturation of Proteins
The process that changes the three dimensional structure of native proteins is
called denaturation of proteins. It can be caused by Change in pH, addition of
electrolyte, heating or addition of solvent like water, alcohol or acetone.
• For example: (i) Coagulation of egg white on boiling, (ii) curdling of milk
which is caused due to the formation of lactic acid by the lactobacillus
bacteria present in milk
Tests of Proteins
(i) Biuret Test
Protein solution + NaOH + dil. CuSO4 → pink or violet colour.