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Dr. P. Suganya
Assistant Professor
Department of Biotechnology
Sri KaliswariCollege (Autonomous)
 Physical Properties
 Chemical Properties
 Amino acids are colorless, crystalline solid.
 All amino acids have a high melting point greater than
200o
 Solubility: They are soluble in water, slightly soluble in
alcohol, and dissolve with difficulty in methanol,
ethanol, and propanol. R-group of amino acids and pH
of the solvent play important role in solubility.
 On heating to high temperatures, they decompose.
 All amino acids (except glycine) are optically active.
 Peptide bond formation: Amino acids can connect
with a peptide bond involving their amino and
carboxylate groups.
 Zwitterionic property
A zwitterion is a molecule with functional
groups, of which at least one has a positive and
one has a negative electrical charge. The net
charge of the entire molecule is zero. Amino
acids are the best-known examples of
zwitterions. They contain an amine group (basic)
and a carboxylic group (acidic).
 Amphoteric property
Amino acids are amphoteric in nature that is
they act as both acids and base due to the two
amine and carboxylic groups present.
 Ninhydrin test
When 1 ml of Ninhydrin solution is added to a 1 ml protein solution and
heated, the formation of a violet color indicates the presence of α-amino
acids.
 Xanthoproteic test
The xanthoproteic test is performed for the detection of aromatic amino
acids (tyrosine, tryptophan, and phenylalanine) in a protein solution.The
nitration of benzoid radicals present in the amino acid chain occurs due
to a reaction with nitric acid, giving the solution yellow coloration.
 Reaction with Sanger’s reagent
Sanger’s reagent (1-fluoro-2, 4-dinitrobenzene) reacts with a free amino
group in the peptide chain in a mild alkaline medium under cold
conditions.
 Reaction with nitrous acid
Nitrous acid reacts with the amino group to liberate nitrogen and form
the corresponding hydroxyl.
 In particular, 20 very important amino acids are crucial for life as they
contain peptides and proteins and are known to be the building blocks
for all living things.
 The linear sequence of amino acid residues in a polypeptide chain
determines the three-dimensional configuration of a protein, and the
structure of a protein determines its function.
 Amino acids are imperative for sustaining the health of the human body.
 They largely promote the:
Production of hormones
• Structure of muscles
• Human nervous system’s healthy functioning
•The health of vital organs
• Normal cellular structure
 The amino acids are used by various tissues to synthesize proteins
and to produce nitrogen-containing compounds (e.g., purines,
heme, creatine, epinephrine), or they are oxidized to produce
energy.
 The breakdown of both dietary and tissue proteins yields nitrogen-
containing substrates and carbon skeletons.
 The nitrogen-containing substrates are used in the biosynthesis of
purines, pyrimidines, neurotransmitters, hormones, porphyrins,
and nonessential amino acids.
 The carbon skeletons are used as a fuel source in the citric acid
cycle, used for gluconeogenesis, or used in fatty acid synthesis.
 https://microbenotes.com/amino-acids-
properties-structure-classification-and-
functions/

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PROPERTIES OF AMINOACIDS.pptx

  • 1. Dr. P. Suganya Assistant Professor Department of Biotechnology Sri KaliswariCollege (Autonomous)
  • 2.  Physical Properties  Chemical Properties
  • 3.  Amino acids are colorless, crystalline solid.  All amino acids have a high melting point greater than 200o  Solubility: They are soluble in water, slightly soluble in alcohol, and dissolve with difficulty in methanol, ethanol, and propanol. R-group of amino acids and pH of the solvent play important role in solubility.  On heating to high temperatures, they decompose.  All amino acids (except glycine) are optically active.  Peptide bond formation: Amino acids can connect with a peptide bond involving their amino and carboxylate groups.
  • 4.  Zwitterionic property A zwitterion is a molecule with functional groups, of which at least one has a positive and one has a negative electrical charge. The net charge of the entire molecule is zero. Amino acids are the best-known examples of zwitterions. They contain an amine group (basic) and a carboxylic group (acidic).  Amphoteric property Amino acids are amphoteric in nature that is they act as both acids and base due to the two amine and carboxylic groups present.
  • 5.  Ninhydrin test When 1 ml of Ninhydrin solution is added to a 1 ml protein solution and heated, the formation of a violet color indicates the presence of α-amino acids.  Xanthoproteic test The xanthoproteic test is performed for the detection of aromatic amino acids (tyrosine, tryptophan, and phenylalanine) in a protein solution.The nitration of benzoid radicals present in the amino acid chain occurs due to a reaction with nitric acid, giving the solution yellow coloration.  Reaction with Sanger’s reagent Sanger’s reagent (1-fluoro-2, 4-dinitrobenzene) reacts with a free amino group in the peptide chain in a mild alkaline medium under cold conditions.  Reaction with nitrous acid Nitrous acid reacts with the amino group to liberate nitrogen and form the corresponding hydroxyl.
  • 6.  In particular, 20 very important amino acids are crucial for life as they contain peptides and proteins and are known to be the building blocks for all living things.  The linear sequence of amino acid residues in a polypeptide chain determines the three-dimensional configuration of a protein, and the structure of a protein determines its function.  Amino acids are imperative for sustaining the health of the human body.
  • 7.  They largely promote the: Production of hormones • Structure of muscles • Human nervous system’s healthy functioning •The health of vital organs • Normal cellular structure  The amino acids are used by various tissues to synthesize proteins and to produce nitrogen-containing compounds (e.g., purines, heme, creatine, epinephrine), or they are oxidized to produce energy.  The breakdown of both dietary and tissue proteins yields nitrogen- containing substrates and carbon skeletons.  The nitrogen-containing substrates are used in the biosynthesis of purines, pyrimidines, neurotransmitters, hormones, porphyrins, and nonessential amino acids.  The carbon skeletons are used as a fuel source in the citric acid cycle, used for gluconeogenesis, or used in fatty acid synthesis.