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Protein PDF
Protein PDF
Decarboxylation reaction:
To form primary amines
e.g Histidine Histamine.
Tryptophan Tryptamine.
Serine Ethanolamine.
C- Reaction due to both NH2
and COOH group
Amino acids condense with each other by COOH group
at one amino acid with NH2 of other amino acid to
form peptide bond. If 3 amino acids condense together
they form tripeptide .
D-Reactions due to radical R:
According to the side chain amino acids give colour
reaction as :
- sulfur test for sulfur containing a.a.
- Xanthoproteic test for aromatic a.a.
- Rosenheim test for tryptophan (indol ring).
- Millon’s test for phenol group as tyrosine.
- Ninhydrin reaction :all amino acids give blue
colour except proline which give yellow colour.
PROTEIN CHEMISTRY
Definition
Proteins are organic complex nitrogenous
compounds of high molecular weight, formed of C, H,
O, N [N= 16%]. They are formed of a number of amino
acids linked together by peptide linkage [-CO-NH-].
The carboxylic group of the first amino acid units with
the amino group of the second amino acid and so on.
Biological importance of
proteins
They provide the body with nitrogen, sulfur, and some vitamins.
Formation of enzymes and protein hormones.
Formation of supporting structures in the body as bone, cartilage, skin,
nails, hair and muscles.
They enter in the formation of buffer system of the blood.
They enter in the formation of haemoglobin
They include plasma proteins, which carry hormones, minerals and
lipids (in the form of lipoprotein complex).
They enter in formation of antibodies (immunoglobulins).
General properties of proteins
Proteins are substances of high molecular weight.
Proteins form colloidal solution and having its
same properties as:
Tyndall effect & Brownian movement
Proteins are non dialyzable due to their large molecules.
Proteins are amphoteric which liable to react with acid and
alkali. Each protein has its own isoelectric point. Protein acts
as a buffer solution which resists the change of its pH by
addition of acid or alkali.
•Denaturation
Denaturation of protein
it is a change in native state (physical, chemical, and
biological properties) of proteins without destruction of
their peptide linkages ,but destruction of secondary bonds
leading to unfolding protein molecule.
Denaturating agents:
Physical: High temperature, high pressure, X-ray,
ultraviolet rays- mechanical agitation.
Chemical: Strong acids, strong alkalies, organic
solvents, heavy metals.
Results of denaturation:
Physical:
Decrease solubility, Iincrease viscosity and can not be
crystallized.
Chemical:
Unfolding of the protein molecule.
Biological:
Loss of activity, if it is hormone or enzyme.