Amino acids
and its types
Definition and General Formula
Amino acids
are the basic building blocks of proteins. Amino acids are bifunctional
(polyfunctional) organic acids having both an acidic carboxyl group (-COOH) and a basic amino group (-NH2 or >NH) along with distinct side chain R (which is
different for different amino acids). Almost all the naturally occurring amino
acids are a-amino acids in which amino group is attached to a-carbon atom (relative to the carboxyl group). They
have following general formula:
Where R
may be hydrogen, a straight or branched chain alkyl group or an aryl group.
The amino group in amino acids may
be present at any carbon atom other than that of carboxyl group containing
carbon (i.e. a–
carbon). Based on whether the amino group is present on the a, β or γ -
carbon atom relative to the carboxyl group, amino acids are referred to as a, β and γ–amino
acids respectively.
Bio-medical Importance of Amino Acids
1.
|
Protein
synthesis
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|
2.
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Hormones
synthesis
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3.
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Energy
Source
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4.
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Regulation
of metabolism
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Types of Amino Acids based on their acidity or alkanity
1.
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Neutral
amino acids
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;
|
contain
one –NH2 & one –COOH group.
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e.g.
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Glycine,
alanine, Valine, Leucine
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2.
|
Acidic amino acids
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;
|
contain
more than one –COOH groups.
|
e.g.
|
Aspargine,
Glutamine
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3.
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Basic amino acids
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;
|
contain
more than one –NH2 groups
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e.g.
|
Lysine, Arginine.
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Essential
Amino acids and Non-essential
Amino Acids
About 20
amino acids have been identified as the constituents of most of the animal and
plant proteins. Out of 20 amino acids which are required for protein synthesis,
the human body can synthesize only 10 and such amino acids are called
Non-essential amino acids. e.g. Glycine, alinine, proline, aspartic acid,
glutamic acid, tyrosine, serine, cysteine, aspargine.
The ten amino
acids that are not synthesized by human body and hence are needed to be
provided in the diet for proper health and growth are called Essential Amino
Acids. [They are 10 for infants and 8 for adult human being]. They
include Valine, Leucine, Isoleucine, Lysine, Methionine, Threonine,
Arginine, Tryptophan, Phenylalanine, and Histidine (last two are needed for
infants).
Zwitterion
The dipolar but overall electrically
neutral charged ion with positive as well as negative ends within the same
molecule is termed as Zwitterion (German; two ions). The dipolar ionic
structure is also called internal salt. All a–amino
acids exist largely as dipolar ionic forms or Zwitterions in solution that is
formed when the proton goes from the acidic carboxylic group (on ionization) to
basic amino group (Lewis base).
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Due to the Zwitter ions form, amino
acids are soluble in water but insoluble in organic solvents. The Zwitterion
formation makes amino acids amphoteric and allows them to donate or accept
proton from the medium or solvent in which they are dissolved.
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Peptide
Linkage
The
acid-amide (-CO -NH -) bond through which amino acids are linked in
proteins by eliminating a water molecule is called Peptide Linkage. This
linkage is formed by the removal of a water molecule b/w an -NH2 group of an amino acid and -COOH group of another. The product formed from
condensation of two amino acids containing a single peptide linkage is called
Dipeptide. The product formed from condensation of three amino acids containing
two peptide bonds is called Tripeptide.
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