PROTEINS
Proteins are very large molecules composed of basic units called amino acids. Proteins contain
carbon, hydrogen, oxygen, nitrogen, and sulfur.
Protein molecules are large, complex molecules formed by one or more twisted and folded
strands of amino acids. Proteins are highly complex molecules that are actively involved in the
most basic and important aspects of life. These include metabolism, movement, defense, cellular
communication, and molecular recognition.
Functions of Proteins
Positive negative attractions between different atoms in the long amino acid strand cause it to
coil on itself again and again to form its highly complex shape. Folded proteins may combine
with other folded proteins to form even larger more complicated shapes.
The folded shape of a protein molecule determines its role in body chemistry. Structural proteins
are shaped in ways that allow them to form essential structures of the body. Collagen, a protein
with a fibre shape, holds most of the body tissues together. Keratin, another structural protein
forms a network of waterproof fibres in the outer layer of the skin.
Functional proteins have shapes that enable them to participate in chemical processes of the
body. Functional proteins include some of hormones, growth factors, cell membrane receptors,
and enzymes.
Sources:
Classification of Proteins
Protein molecules are large, complex molecules formed by one or more twisted and folded
strands of amino acids. Each amino acid is connected to the next amino acid by covalent bonds.
Primary (first level) – Protein structure is a sequence of amino acids in a chain.
Secondary (secondary level) – Protein structure is formed by folding and twisting of the amino
acid chain.
Tertiary (third level) – Protein structure is formed when the twists and folds of the secondary
structure fold again to form a larger three dimensional structure.
Quaternary (fourth level) – Protein structure is a protein consisting of more than one folded
amino acid chain.
Proteins can bond with other organic compounds and form “mixed” molecules. For example,
glycoproteins embedded in cell membranes are proteins with sugars attached. Lipoproteins are
lipid-protein combinations.
SIMPLE PROTEIN:
On hydrolysis gives only amino acids , Examples: 1- Albumin and globulins: present in egg,
milk and blood. They are proteins of high biological value i.e. contain all essential amino acids
and easily digested. Albumin is a protein made by the liver. It makes up about 60% of the total
protein in the blood and plays many roles. Albumin keeps fluid from leaking out of blood vessels
and transports hormones, vitamins, drugs, and substances like calcium throughout the body
Globulins The globulins are a family of globular proteins that have higher molecular weights
than albumins and are insoluble in pure water but dissolve in dilute salt solutions. Types of
globulins: α1 globulin: e.g. antitrypsin α2 globulin: e.g. hepatoglobin: protein that binds
hemoglobin to prevent its excretion by the kidney
CONJUGATED PROTEIN:
Conjugated proteins They are combinations of protein with a non-protein part, called prosthetic
group Conjugated proteins may be classified as follows
1-Glycoproteins: These are proteins combined with carbohydrates. Hydroxyl groups of serine or
threonine and amide groups of asparagine and glutamine form linkages with carbohydrate
residues. Blood group antigens and many serum proteins are glycoproteins.
2- Lipoproteins: These are proteins loosely combined with lipid components. They occur in
blood and on cell membranes.
3- Nucleoproteins: These are proteins attached to nucleic acids, e.g. Histones. The DNA carries
negative charges, which combines with positively charged proteins
. 4- Chromoproteins: These are proteins with coloured prosthetic groups. Hemoglobin (Heme,
red);Flavoproteins (Riboflavin, yellow) are some examples of chromoproteins.
Derived Proteins:
1. As the name suggests, the derived proteins are the derivatives of the proteins.
2. These proteins are made up of simple or conjugated proteins that have been partially
hydrolyzed by acids, enzymes, or alkalies.
3. In the process of formation of proteins, the intermediate chemicals are also formed in
descending order of complexity.
Examples of derived proteins:
1. Examples of derived proteins are proteases, peptones, and peptides.
2. These are formed during the digestion of proteins.
PROPERTIES:
Physical properties Major physical properties of proteins include
: Colour and Taste : Proteins are usually colourless and tasteless, homogeneous and crystalline
. Shape and Size : They range in shape from simple crystalloid spherical structures to long
fibrillar structures. Two distinct shapes have been characterized.
Denaturation: This is a process that involves the disruption of the secondary and tertiary
structures of the protein, leading to the loss of biological activity. Often, denaturation is followed
by coagulation, a process in which denatured protein molecules form large aggregates which
precipitate from solution.
Amphoteric nature: Just like amino acids, proteins are amphoteric in nature, i.e. they act as
both acids and alkalies. Proteins migrate in an electric field and the direction of migration
depends upon the net charge carried by the molecule, which is influenced by the pH value. Each
protein has a fixed value of isoelectric point (pI) at which it will not move in an electric field.
REACTION OF PROTEINS:
Biuret test: Compounds containing peptide bonds produce a characteristic purple colour when
treated with an alkaline 0.2% copper sulfate solution (Biuret reagent). This reaction is named
'Biuret reaction' as it is also given by the compound, Biuret. The colour deepens as the number of
peptide bonds is increased and the proteins produce a deep blue-violet colour due to the probable
formation of a coordination complex.
Xanthoproteic test: On boiling proteins with conc. HNO3, yellow colour develops due to the
presence of benzene rings. This reaction is due to the nitration of the phenyl rings (present in tyr,
phe, and trp) to yield yellow substitution products, which turns orange upon addition of alkali.