Protiens and Amino Acids
Protiens and Amino Acids
Protiens and Amino Acids
The word “protein” Originates from the Greek word “proteios” which means of prime
importance or holding first place.
Importance of proteins
Proteins are crucial for enzymatic activity, structural support, and transport in the
body.
Play a vital role in immune response and cell signaling.
Can be catabolize to supply energy
Several hormones are proteins in nature.
Some proteins present in cell membrane, cytoplasm and nucleus of the cell act as
receptors.
Storage proteins bind with specific substance and store them, e.g. Iron is stored as ferritin
Composition of proteins
In addition to C, H, and O which are present in carbohydrates and lipids, proteins also
contain N which is about16% of its weight.
Amino acids are the building blocks of proteins (which are large molecules with high
molecular weight about 5000 to 25,000,000).
They are organic compounds containing amino group (-NH2) and a carboxylic
group (COOH).
Proteins are the unbranched polymers of L-a-aminoacids.
General formula
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Classification of Amino acids:
Amino acids are classified into 3 groups depending on their reaction in solution
A. Neutral Amino Acids
B. Acidic Amino Acids
C. Basic Amino Acids
B. Acidic amino acids: These amino acids have 2–COOH groups and 1 – NH group. They are
there for mono amino di carboxylic acids.
1. Aspartic acid
2. Glutamine
3. Asparagine
4. Glutamic Acid
C. Basic amino acids: This class of amino acids consists of those amino acids which have
2
1–COOH group and 2–NH2 groups. Thus they are diamino monocarboxylic acids.
1. Arginine
2. Lysine
3. Histidine
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Classification of Proteins
B. Conjugated proteins:
These are proteins which in addition to amino acids contain non protien group (prosthetic
group) in their structure. Sub classification
These are further sub classified into following:
a) Nucleoproteins The nucleoproteins are compounds made up of simple basic proteins such as
protamine or histone with Nucleic Acids as the prosthetic group.
b) Deoxyribonucleo proteins:: It contain DNA as prosthetic Group, are found in nuclei
mitochondria and chloro-Plasts.
c) Ribonucleoproteins: It occurs in nucleoli and ribosome Granules. They have RNA as
prosthetic group.
i. Examples: Nucleo histone and neucleo protamine.
d) Glycoproteins: Glycoproteins are the proteins with carbohydrate moiety as the prosthetic group.
Glycoproteins include mucins.
e) Chromoproteins: These are the proteins with phosphoric acid as organic Phosphate but not the
phosphate containing substances
f) Lipoproteins: The lipoproteins are formed in combination with lipids as their prosthetic group.
As the name indicates, they contain a metal ion as their prosthetic group.
C. Derived Protiens
These are protiens formed by native protein by the action of heat, physical for cesor
chemical factors
Sub-classificaton:
Primary Derived proteins
Secondary Derived proteins
Denatured or coagulated
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General Properties of Proteins
1. Taste: Tasteless.(protein derived) are bitter in taste.
2. Odour: Odorless on heating turn brown and give odor of burning feather.
3. Molecular weight: Large molecular weight thus are macro molecules e.g. Serum albumin
(6900), Hemoglobin(67000)
4. Viscosity: Viscosity is closely related to molecular shape.long molecules more viscous than
globular proteins.
5. Hydration: Polar groups of proteins hydrated in presence of water.
when electrolytes, alcohol or sugar added they dehydrate protein and precipitate it from
solution.
6. Heat coagulation of protein: During coagulation protein denatured.
Coagulation is maximum at isoelectric pH of protein.
7. Amphoteric nature: Proteins have amino acids which on ionization produce anion and
cation. Depending upon pH acts as proton donor or proton acceptor,
Thus protein act both as an acid or base.
.At iso-electric pH protein exist as zwitter ion, equal numbers of positive and negative charges.
So at isoelectric pH charge on protein is zero.
8. Precipitation of Protein: Proteins can be precipitated by a number of +ve and-ve ions.
By +ve ions: Such as Zn+², Ca+2, Fe+3 (heavy metals) precipitate protein at pH
alkaline to its isoelectric pH.
By -ve ions: Negative ions combine with proteins at pH Acidic to its isoelectric pH.
-NH2 group is the reacting group in this case.
9. Colour reaction: Protein produce colour in certain reactions e.g.
Millions test: give white ppt (tyrosine of protein)
Sakaguchi test: give red color ppt (arginine of protein)
Sullivan reaction: give reddish colour.
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Properties of Amino Acids:
Physical Properties
1. Amino acids are colorless, crystalline solids.
2. All amino acids have a high melting point greater than 200o
3. 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.
4. On heating to high temperatures, they decompose.
5. All amino acids (except glycine) are optically active.
6. Peptide bond formation: Amino acids can connect with a peptide bond involving
their amino and carboxylate groups. A covalent bond formed between the alpha-
amino group of one amino acid an danalpha-carboxylgroup of other forming -CO-
NH-linkage. Peptide bonds are planar and partially ionic.
Chemical Properties
1. 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.
2. Ninhydrintest:
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.
3. 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.
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5. Peptide linkage
A peptide linkage is a chemical bond formed between two molecules when the carboxyl group of
one molecule reacts with the amino group of the other molecule, releasing a molecule of water
(H2O). for exampe
Valine and alanine can form the dipeptide valyalanine through the formation of a peptide
bond.
Example:
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