Documenti di Didattica
Documenti di Professioni
Documenti di Cultura
acid
Nutritional : either essential or non essential amino
acids
Metabolic: either glucogenic or ketogenic amino acids
Charge and polarity of side chain
ii Nutritional Classification:
1) essential amino acids:
Phenylalanine , Treptophan,Histidin .
Methionine , Threonine .
Leucine , Valine , Isoleucine.
Arginine, Lysine .
2- Hydrophilic polar:
a- Uncharged polar amino acid as serine,threonine
b- Charged polar amino acids
Positively charged
Negatively charged
Zwittern ion:
It is the dipolar ion of amphoteric compounds (amino
acid and proteins) produced when the pH of the
medium is at the I.E.P. It carries both +ve and ve
charges and thus it is electrically neutral (does not
move in electric field).
Decarboxylation reaction:
To form primary amines
e.g Histidine Histamine.
Tryptophan Tryptamine.
Serine
Ethanolamine.
reaction as :
- sulfur test for sulfur containing a.a.
- Xanthoproteic test for aromatic a.a.
- Rosenheim test for tryptophan (indol ring).
- Millons 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,
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:
Results of denaturation:
Physical:
Folloculation of proteins
It
is a precipitation of denaturated
protein at its I.E.P.
This folloculation is dissolved again by
changing pH from the I.E.P by
addition of acid or alkali (reversible).
Coagulation of prteins
Boiling of the folloculated protein changing
it to coagulum.
This coagulum can not dissolved again even
by changing the pH (irreversible).
Precipitation of proteins
Proteins are precipitated from solution by many ways:
At I.E.P.
By high concentrations of neutral salts as ammonium
sulfate, Mg sulfate, Na chloride.
By heavy metals e.g. silver nitrate, lead acetate.
By strong acids e.g. trichloro acetic acid (TCA),
phosphotungestic acid, picric acid.
By organic solvents which are miscible with H2O e.g.
ethyl alcohol, methyl alcohol, acetone.
Fractionation of proteins
Precipitation by neutral salts
Electrophoresis:
It is the migration of proteins in an electric field.
Classification of proteins
Prpteins can be classified on the basis of their
solubility, shape,biological functions,or chemical
composition
1-Classification of proteins according to their
solubility:
Proteins soluble in H2O,or other biological solvents
(Albumin globulin- Histones Protamin - prolamin
glutelins)
Proteins not soluble in most protein solvents
[albuminoids] as nail and hair.
hormones
Structural proteins: collagen
Protective proteins: clotting factors , immunoglobulins
Transport proteins: hemoglobin , plasma lipoproteins
Motile proteins: actin, tubulin
albuminoids(scleroproteins).
albuminoids (scleroproteins)
They are fibrous proteins.
Insoluble in H2O, dilute acids and alkali, and all
neutral solvents.
gelatin.
IMMUNOGLOBALINS (IGs)
Globulins are mainly formed in reticuloendothelial system in macrophages and
lymphocytes.
Immune system is divided into :
B-cells (Bone marrow): concerned with circulating
humeral antibodies.
T-cells (Thymus glands): concerned with cell mediated
immune response as graft rejection, hyypersensitivity
reactions and defense against malignant cells and viral
infection.
Lipoproteins:
Protein conjugated with lipids either [phospholipids-
Phosphoproteins:
Protein conjugated with phosphoric acid thruogh
Metalloproteins
Proteins conjugated with metals e.g.
Ceruloplasmin = protein + Cu.
Insulin = protein + zinc.
Chromoproteins:
Hemoglobin containing Fe-porphyrin (red color).
Chlorophyll containing Mg-porphyrin (green color).
Flavoproteins: These are enzymes containing FMN,
Nucleoproteins:
Proteins conjugated with nucleic acids e.g. Histone
associated with DNA in chromosomes.
C-Derived proteins
These are the denaturated or hydrolytic products of
either simple or conjugated proteins.
1- Primary protein derivatives:
These results from alteration of proteins from its native
Proteoses:
Peptones:
Peptides:
Resulting from further hydrolysis of peptones.
Amino acids
Structure of proteins:
Proteins are formed of a large number of
-pleated Sheets
-sheets are composed of 2 or more different regions of
stretches of at least 5-10 amino acids. The folding of
the polypeptide backbone aside one another to form sheets is stabilized by H-bonding between amide
nitrogens and carbonyl carbons. -sheets are said to be
pleated. This is due to positioning of the -carbons of
the peptide bond which alternates above and below
the plane of the sheet.
- Loop sheets:
Half of the residues in a typical globular protein are
2- Hydrophobic Forces:
Proteins are composed of amino acids that
contain either hydrophilic or hydrophobic
R-groups. It is the nature of the interaction
of the different R-groups with the aqueous
environment that plays the major role in
shaping protein structure.
The hydrophobicity of certain amino acid Rgroups tends to drive them away from the
exterior of proteins and into the interior.
This driving force restricts the available
conformations into which a protein may
fold.
3- Electrostatic Forces:
Formed between oppositely charged groups in the side
5- Disulphide bonds:
Protein folding
Protein folding is the process by which a string
of amino acids (the chemical building blocks
of protein) interacts with itself to form a
stable three-dimensional structure during
production of the protein within the cell. The
folding of proteins thus facilitates the
production of discrete functional entities,
including enzymes and structural proteins,
which allow the various processes associated
with life to occur
Protein misfolding
Under favorable conditions, most proteins have no