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Proteins are a kind of substance that has presence of amino acids, carbon, nitrogen, hydrogen, oxygen, compounds. In some cases proteins also do contain sulphur. They are mainly found in food, for example, meat, beans, eggs, etc. Proteins are the building blocks of life and form 60% of dry cells in the body and form the fundamental basis of structure and functions of life. Chief sources of protein are eggs, pulses, fish, meat, milk and other milk products which in turn help in growth and maintenance of the body. “Proteios” is a Greek word meaning something which is of prime importance and the term ‘protein’ is derived from it.
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Key Terms: Protein, compounds, unit of life, cells, amino acids, peptide bond, amino acids, carbon, nitrogen, hydrogen, oxygen, sulphur
Building Blocks
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Amino acids are the basic blocks which form protein molecules formed by linking the carboxyl group (-COOH) of one amino acid with the amino group (– NH2) of another amino acid releasing a molecule of water (H2O). The resultant bond formed is called peptide bond and can belong to the α, β, γ, δ category. Hydrolysis of proteins leads to generation of α-amino acids. Amino acids are usually colourless, crystalline solids. These are water-soluble, high melting solids and act like salts rather than simple amines or carboxylic acids.Depending upon the relative position of amino group with respect to carboxyl group dipeptide, tripeptide, and polypeptide linkages are formed. When two amino acids are linked together a dipeptide linkage is formed. While three, four, five and six amino acid linkages lead to generation of tripeptides, tetra peptide, penta peptide & hexa peptide respectively. On the other hand, more than ten amino acid linkages produce polypeptides with more than 100 amino acid residues. They have molecular mass greater than 10,000, or less than 100 amino acid remains. They also have a precise shape and are referred to as proteins. Amino acids may be of three different kinds: acidic, basic or neutral. The nature of the amino acid depends upon the respective number of amino and carboxyl groups present in their molecule. When amino and carboxyl groups share equal numbers the amino acid is treated as neutral, while greater number of amino than carboxyl groups makes it basic and more carboxyl groups as compared to amino groups generate acidic properties. Essential amino acids are those which cannot be synthesized in the body and must be obtained through diet.
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| Chapter Related Concepts | ||
|---|---|---|
| Carbohydrate Metabolism | RNA and DNA | |
| Cellulose | Fats and Oils | Sucrose |
Classification of Proteins
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Proteins can be classified into various categories on the basis of the following parameters:
- Shape
- Constitution
- Nature of molecules
Based on shape, proteins can be further classified into
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Fibrous protein (Scleroprotein)
These proteins are insoluble in water and are resistant to proteolytic enzymes and are coiled and exist in threadlike structures to form fibres. e.g. collagen, actin, and myosin, keratin in hair, claws, feathers, etc These proteins are mainly available in animals.
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Globular proteins
These are water soluble proteins, made up of polypeptides that are coiled about themselves to form oval or spherical molecules e.g. albumin, insulin, and hormones like oxytocin, etc.
Based on constitution, proteins can be further classified into
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Simple proteins
These types of proteins have amino acids as their only constituent e.g. albumins, globulins, prolamins, etc.
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Conjugated proteins
These kinds of proteins are complex in nature and are fused with the characteristics of a non–amino acid substance known as the prosthetic group. These can be nucleoproteins, mucoproteins, glycoproteins, chromoproteins, lipoproteins, metalloprotein, phosphoprotein depending upon the percentage of combination of proteins and nucleic acid/ proteins and Carbohydrates/ proteins and coloured pigments/ proteins and lipids/ proteins and metal ions/ proteins and phosphate group.
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Derived proteins
Hydrolysis of proteins by acids, alkalies or enzymes, lead to generation of derived proteins.
Based on nature of molecules, proteins can be further classified into
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Acidic proteins
These proteins exist as anions and are rich in acidic amino acids. e.g. blood groups.
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Basic proteins
These proteins exist as cations and are rich in basic amino acids e.g. lysine, arginine etc.
Structure of Proteins
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Proteins are polymers of α-amino acids connected to each other by peptide bond or peptide linkage. This linkage is an amide formed between the –COOH group and –NH2 group. The reaction between the amino group of one molecule with the carboxyl group of the other leads to the generation of peptide bonds –CO–NH- with the release of water molecules. Peptides can be dipeptide, tripeptide, and polypeptide depending upon the relative position of the amino group with respect to the carboxyl group. Polypeptides that have fewer amino acids are known as proteins. They have a well structured conformation of the protein such as insulin which contains 51 amino acids. Amino acids are substituted methane whose four valencies are occupied by hydrogen, amino group, carboxyl group and the remaining one by a variable R- group. The R group controls the variety of amino acids, out of which 20 are found in a polypeptide chain. These properties control the ultimate structure of protein.
Structure of protein can be classified into primary, secondary, tertiary and quaternary based on ascending order of their complexity.
- Secondary structure of protein: Secondary structure of proteins refers to the shape where a long polypeptide chain exists.
- Tertiary structure of protein: Tertiary structure of proteins refers to further folding of the secondary structure. Hydrogen bonds, disulphide linkages, van der Waals and electrostatic forces of attraction stabilize the structure of this protein.
- Quaternary structure of protein: Quaternary structure deals with spatial arrangement of two or more polypeptide chains relative to one another.
Functions of Protein
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Protein plays a crucial role in proper functioning of body. Few of the prominent functions of protein are:
Enzymes – Enzymes regulate different biochemical reactions occurring in the body. For instance digestive enzymes which are composed of protein help in digestion.
Movement – Contraction and expansion of muscles for making movement is controlled by myosin, a protein found in muscles.
Structure and Support – Proteins are essential components of various structures in the cell and tissues Growth of hair, nails and horns in animals is attributed to keratin, a structural protein found in animals.
Protective – Antibodies play a vital role in protecting our body against antigens and pathogens. Proteins are the main constituent of these antibodies.
Hormonal regulation – Hormones which are composed of proteins play vital role in regulating muscle mass, sex hormones, growth and development.
Cellular communication – Cells communicate with one another via receptors present on the surface of cells. These receptors are made of proteins.
Act as a messenger – These proteins function as the chemical messengers, which help in the communication between the cells, tissues, and organs.
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Sample Questions
Ques. What is the end product when lactose undergoes hydrolysis?(1 mark)
Ans. P-D-galactose and p-D-glucose is the end product of hydrolysis.
Ques. Name the linkage that joins two amino acids.(1 mark)
Ans. It is the peptide linkage that joins two amino acids.
Ques. Name the bases which are present in DNA.(2 marks)
Ans. The four bases include:
- Adenine
- Guanine
- Cytosine
- Thymine
Ques. Explain amino acid.(1 mark)
Ans. Amino acids are usually colourless, crystalline solids. These acids are water-soluble, is a high melting solids and act like salts instead of simple amines or carboxylic acids.Depending upon the relative position of amino group with respect to carboxyl group dipeptide, tripeptide, and polypeptide linkages are formed.
Ques. Name the different structure of proteins.(2 marks)
Ans. The different structure of protein includes:
- Primary structure
- Secondary structure
- Tertiary structure
- Quaternary structure.
Previous Year QuestionsQues 1. Differentiate between the following: Ans. (i) Amylose and Amylopectin
(ii) Peptide linkage and Glycosidic linkage
(iii) Fibrous proteins and Globular proteins.
Ques 2. Define the following terms: Ans. (a) Invert sugar - Invert sugar is an amalgamation of the glucose and fructose extracted as a result of sucrose hydrolysis. Sucrose is dextrorotatory in nature but, post hydrolysis it gives out an amalgamation of dextrorotatory glucose and levorotatory fructose which exceeds in magnitude, therefore the whole mixture turns out to be levorotatory and the mixture extracted is known as invert sugar. (b) Native protein - The protein that can be found in a biological system and has a special 3-dimensional structure and activity that can be termed as biological is known as native protein. (c) Nucleotide - Nucleotides are known to be the building blocks of DNA/RNA. They have the pentose sugar moiety joined to a nitrogenous base at a position V and a molecule of the phosphoric acid at a position 5’. Example:
Ques 3. (a) What is the product of hydrolysis of maltose? Ans. (a) The maltose gives rise to two molecules of D-glucose on its hydrolysis.
(b) The protein’s α-Helix structure is balanced by the hydrogen bonds that take between the -NH group of every amino acid and -COOH group of amino acid at an adjacent turn.
Ques 4. (a) Write the product when D-glucose reacts with conc. HNO3. Ans. (a) The D-Glucose gives out saccharic acid on oxidation, a dicarboxylic acid on reacting with the nitric acid.
(b) When both the acidic carboxylic group as well as the basic amino group are present in the similar molecule the amino acids give an amphoteric behaviour. In the basic medium the carboxylic group might end up losing a proton and in the acidic medium the amino group might end up adding a proton. (c) When it comes to the α-helix structure the polypeptide chain tends to form every plausible hydrogen bond by forming a helix along with the -NH group of every amino acid left-over gets bonded with hydrogen to the -C = O of an adjacent rotation of the helix (intramolecular bonding). Whereas in the - structure every peptide chain is elongated to the almost maximum extension possible. Then they are placed beside each other which are fastened together by the intermolecular hydrogen bonds. Ques 5. Give one example each for brous protein and globular protein. (2016) Ans. one example each for brous protein and globular protein are:
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