ASSIGNMENT

BIOMOLECULES

(SUBJECT - CHEMISTRY)

SUBMITTED BY :-
Manav Bindal
CLASS - XII SCIENCE
INTRODUCTION:

Biomolecules are complex organic compounds that govern the common activities
of living organisms. Carbohydrates, proteins, nucleic acids, lipids, and other
complex biomolecules make up living systems. Furthermore, simple molecules
such as vitamins and mineral salts play an important role in the functions of
organisms.
CARBOHYDRATES:

Also known as saccharides, Carbohydrates are organic compounds primarily synthesized by plants.
- Common examples include cane sugar, glucose, and starch.
- Historically named hydrates of carbon, their general formula is Cx(H2O)y.
● Example: Glucose (C6H12O6) fits this formula.
● Exceptions exist, such as:
○ Acetic acid (CH3COOH) fits the formula but is not a carbohydrate.
○ Rhamnose (C6H12O5) is a carbohydrate but does not fit the formula.

They are defined as optically active polyhydroxy aldehydes or ketones, or compounds yielding such units
upon hydrolysis.
CLASSIFICATION OF CARBOHYDRATES:

- Carbohydrates are classified based on how they react to hydrolysis.

1. MONOSACCHARIDES:
The simplest carbohydrates, cannot be hydrolyzed into smaller molecules, with the general formula
C H₂ O . Examples include glucose, fructose, and ribose.

Types:
Aldose: Contains an aldehyde group (−CHO), e.g., Glucose.
Ketose: Contains a ketone group (C=O), e.g., Fructose.

Carbon Atoms General Term Aldehyde Ketone

3 Triose Aldotriose Ketotriose
4 Tetrose Aldotetrose Ketotetrose
5 Pentose Aldopentose Ketopentose
6 Hexose Aldohexose Ketohexose
7 Heptose Aldoheptose Ketoheptose

2. OLIGOSACCHARIDES:
Carbohydrates that yield 2-10 monosaccharides on hydrolysis.

Disaccharides: Two monosaccharide units

E.g. Sucrose → Glucose + Fructose

Trisaccharides: Three monosaccharide units.

3. POLYSACCHRIDES:
Large carbohydrates that yield many monosaccharides on hydrolysis, known as non-sugars due to their lack
of sweetness.
- General Formula: (C₆H₁₀O₅) .
Examples:
Starch: Energy storage in plants.
Cellulose: Structural component in plants.
Glycogen: Energy storage in animals.
GLUCOSE:

Found in both free and combined forms in nature, notably in honey, sweet fruits, and ripe grapes (often
called grape sugar). It is a unit of starch, cellulose, and glycogen.

PREPRATION OF GLUCOSE:

- From Sucrose:
Boiling sucrose (C₁₂H₂₂O₁₁) with dilute HCl or H₂SO₄ in an alcoholic solution produces an equal amount of
glucose and fructose.

- From Starch:
Glucose is obtained by hydrolyzing starch (C₆H₁₀O₅) with dilute H₂SO₄ at 393 K and 2-3 atm pressure.

STRUCTURE:

Glucose is an aldohexose, often called dextrose, with the molecular formula C₆H₁₂O₆.
It is a monomer for larger carbohydrates such as starch and cellulose.

REACTIONS:

1. Oxidation:
Oxidizing glucose or gluconic acid with nitric acid produces saccharic acid, indicating the presence of a
primary alcoholic (-OH) group.
2. Reduction:
On heating with HI, glucose reduces to n-hexane (a straight-chain hydrocarbon).

3. Cyanohydrin Formation:
Glucose reacts with hydrogen cyanide to form a cyanohydrin.
4. Oxime Formation:
Glucose reacts with hydroxylamine to form an oxime.

5. Reaction with Phenylhydrazine (Osazone Formation):

Glucose reacts with phenylhydrazine to form osazone, which confirms the presence of two reactive
carbonyl groups. (X = 2)

6. Acetylation:
Glucose pentaacetate forms when glucose reacts with acetic anhydride, confirming the presence of five
–OH groups.
CYCLIC STRUCTURE OF GLUCOSE:

Glucose exists in two crystalline forms, α-D(+)-glucose and β-D(+)-glucose, which differ in the
arrangement of the hydroxyl group on the C1 (anomeric carbon). The α-form crystallizes at 303 K with a
melting point of 419 K, while the β-form crystallizes at 371 K with a melting point of 423 K. In aqueous
solution, both forms interconvert through a process called mutarotation, where their specific rotation
changes over time to an equilibrium value of +52.5°. Glucose forms a six-membered cyclic hemiacetal ring
(pyranose) by reacting the aldehyde group at C1 with the hydroxyl group at C5, explaining why the free
–CHO group is absent. The two forms, α and β, are called anomers. The Haworth structure is used to
represent this stable cyclic form, which predominates in solution.

Pyranose structure is a six-membered cyclic structure of glucose (– or –), in analogy with pyran. Pyran is a
cyclic organic compound with five carbon atoms and one oxygen atom in the ring.
FRUCTOSE:

Fructose is an important ketohexose with the molecular formula C₆H₁₂O₆. It is naturally found in
vegetables, fruits, and honey and can be obtained by the hydrolysis of sucrose, yielding glucose and
fructose. Structurally, fructose contains a ketonic functional group at C2 and has six carbons arranged in a
straight chain. It is a laevorotatory compound and belongs to the D-series, written as D-(–)-fructose.

The cyclic structure of fructose forms when the hydroxyl group at C5 reacts with the ketonic group at C2,
resulting in two cyclic forms. These cyclic forms exhibit properties similar to reducing carbohydrates but
do not show mutarotation.

FISHER PROJECTION -

HOWARTH SRUCTURE -
DISACCHRIDES:

Disaccharides are carbohydrates formed when two monosaccharides join through a glycosidic linkage with
the loss of a water molecule. They are classified as reducing or non-reducing sugars based on whether their
reducing groups (aldehydic or ketonic) are free or bonded.

1. SUCROSE:

Sucrose consists of α-D-glucose and β-D-fructose, linked via a glycosidic bond between C1 of glucose and
C2 of fructose. It is a non-reducing sugar as both reducing groups are involved in the bond. Sucrose is
dextrorotatory, but after hydrolysis, it forms a laevorotatory mixture called invert sugar. It occurs naturally
in fruits and is commercially produced from sugarcane and sugar beets.

2. MALTOSE:

Maltose is made of two α-D-glucose units, with C1 of one glucose linked to C4 of another. The second
glucose has a free aldehyde group, making maltose a reducing sugar.
3. LACTOSE:

Lactose, or milk sugar, is composed of β-D-galactose and β-D-glucose. A glycosidic bond connects C1 of
galactose to C4 of glucose. Lactose is a reducing sugar due to its ability to produce a free aldehyde group at
C1 of glucose.
POLYSACCHRIDES:

Polysaccharides are carbohydrates formed by linking multiple monosaccharide units through glycosidic
linkages. They serve as food storage or structural materials in organisms.

1. STARCH:

Starch is the primary storage polysaccharide in plants, commonly found in vegetables, roots, tubers, and
cereals. It is a polymer of α-glucose and consists of two components:

- Amylose: Constitutes 15-20% of starch, is water-soluble, and has a linear chain of 200-1000
α-D-glucose units linked by C1–C4 glycosidic bonds.

- Amylopectin: Makes up 80-85% of starch, is water-insoluble, and has a branched-chain structure

with C1–C4 glycosidic bonds forming the chain and C1–C6 glycosidic bonds forming branches.

Starch is a non-reducing saccharide, meaning it does not react with Tollen’s reagent or Fehling’s solution.

2. CELLULOSE:
Cellulose is the most abundant organic substance in the plant kingdom, found in the cell walls of plants. It
is composed of β-D-glucose units linked by C1–C4 glycosidic bonds in a straight chain. Cellulose provides
structural support to plants.

3. GLYCOGEN:

Glycogen, often called animal starch, is the primary carbohydrate storage form in animals, found in the
brain, muscles, liver, fungi, and yeast. Its structure resembles amylopectin but is more highly branched,
with glucose units linked by α-1,4 glycosidic bonds and branches formed by α-1,6 glycosidic bonds.
Enzymes break glycogen down into glucose when the body needs energy. Carbohydrates, as essential
biomolecules, serve as a major food source and energy reserve, with starch stored in plants and glycogen in
animals. Cellulose forms the structural framework of plant and bacterial cell walls, while honey is valued
in Ayurveda as an instant energy source. Additionally, carbohydrates are vital raw materials in industries
like paper, textiles, and brewing.
PROTIENS:

Proteins were introduced by Jöns Jakob Berzelius and derived from the Greek word proteios, meaning
"first" or of prime importance. Proteins are essential biomolecules that form the structural and functional
basis of life. They are the most abundant biomolecules in living organisms and are present in every part of
the body.

- Sources: Cheese, milk, pulses, peanuts, etc.

- Function: Proteins are required for body maintenance, growth, and performing various functions
such as enzymes, hormones, and antibodies.

AMINO ACIDS:

Amino acids are organic compounds that contain both a carboxyl group (–COOH) and an amino group
(–NH2). The term α-amino acids refers to amino acids where the amino group is attached to the carbon
next to the carboxyl group.

Formula: General structure of an amino acid:

where R represents the side chain or functional group specific to each amino acid.

Types of Amino Acids:

- Neutral Amino Acids: Equal number of carboxyl and amino groups.

- Basic Amino Acids: More amino groups than carboxyl groups.
- Acidic Amino Acids: More carboxyl groups than amino groups.

Classification of Amino Acids

- Non-Essential Amino Acids: These can be synthesized by the body.

- Essential Amino Acids: These must be obtained from the diet because the body cannot synthesize
them. Deficiency can lead to diseases like Kwashiorkor. Examples include:
● Valine
● Leucine
● Isoleucine
● Lysine
● Threonine
● Phenylalanine
● Methionine
● Tryptophan
● Histidine
● Arginine
CHARACTERISTICS OF AMINO ACIDS:

Amino acids are typically colorless, crystalline solids, water-soluble, and have high melting points.

Zwitterion Formation: In an aqueous solution, the amino group can accept a proton, and the carboxyl group
can lose a proton, resulting in a zwitterion—a dipolar ion that has both a positive and a negative charge but
is overall neutral.

Optical Activity: Except for glycine, all naturally occurring α-amino acids are optically active. They exist
in both "D" and "L" forms, with the L-form being the naturally occurring form.

Peptide Bond: A peptide bond is an amide bond that forms between the carboxyl group of one amino acid
and the amino group of another. This bond is formed by a condensation reaction that releases a water
molecule.

Example: Glycine + Alanine → Glycylalanine (Dipeptide).

Peptides: A peptide is a short chain of amino acids. When more than 10 amino acids are linked, the product
is called a polypeptide.

Peptide Length:

● Dipeptide (2 amino acids)

● Tripeptide (3 amino acids)
● Tetrapeptide (4 amino acids)
● Polypeptide (more than 10 amino acids)

Proteins are long chains (more than 100 amino acids, molecular mass > 10,000 Da).

STRUCTURE OF PROTIENS:

Peptide types;

- Dipeptide: Formed by the combination of two amino acids.

- Tripeptide: Contains three amino acids linked by two peptide bonds.
- Polypeptides: Longer chains of amino acids, often referred to as proteins if their molecular weight
is above 10,000 u and contain more than 100 amino acid residues.
Proteins are classified based on their molecular shape:

- Fibrous Proteins: Insoluble in water, stable to temperature and pH changes. Examples include
keratin (hair) and myosin (muscles).
- Globular Proteins: Soluble in water, typically functional proteins like insulin, hemoglobin, and
antibodies.

N-Terminal and C-Terminal:

- N-terminal is the free amino group end.
- C-terminal is the free carboxyl group end.

Hydrolysis of Proteins:
- Simple Proteins: Yield only amino acids on hydrolysis (e.g., albumins).
- Conjugated Proteins: Contain non-protein groups like nucleic acids or carbohydrates (e.g.,
hemoglobin).
- Derived Proteins: Result from partial hydrolysis of simple proteins (e.g., peptones).

Protein Structure:
- Primary Structure: The specific sequence of amino acids in a polypeptide chain.
- Secondary Structure: Regular folding of the polypeptide chain into structures like alpha helices and
beta-pleated sheets due to hydrogen bonding.
- Tertiary Structure: The three-dimensional folding of the polypeptide chain stabilized by various
interactions like hydrogen bonds, disulfide bridges, and van der Waals forces.
- Quaternary Structure: The arrangement of multiple polypeptide chains in a protein (e.g.,
hemoglobin).
Denaturation of Proteins:
Denaturation occurs when the native structure of a protein is disrupted, causing it to lose biological activity.
Factors such as changes in pH, temperature, salts, or chemicals can alter the protein's three-dimensional
structure by disturbing hydrogen bonds.
Examples:
- Boiling an egg causes albumin to coagulate.
- In cheese formation, lactalbumin (a globular protein) becomes fibrous.

Detection of Proteins:
- Millon’s Test: Produces a white precipitate with millon’s reagent (except tyrosine).
- Xanthoprotein Test: Proteins with tyrosine or phenylalanine give a yellow color with concentrated
HNO₃.
- Ninhydrin Test: Produces a blue-violet color when proteins are boiled with ninhydrin.
- Biuret Test: Proteins in an alkaline solution give a violet color with copper sulfate, due to the
formation of a complex with peptide linkages.
LIPIDS:

Lipids are a diverse group of compounds that are generally insoluble in water. They are primarily
composed of fatty acids, which are carboxyl groups attached to an R group that can be ethyl (–C₂H₅),
methyl (–CH₃), or longer chains of carbon atoms, typically ranging from 1 to 19 carbons. For example,
palmitic acid has 16 carbon atoms, while arachidonic acid contains 20 carbon atoms. Fatty acids can be
classified into saturated fatty acids, which do not contain double bonds, and unsaturated fatty acids, which
contain one or more C=C double bonds. Another important lipid is glycerol, a trihydroxy propane, which,
when esterified with fatty acids, forms monoglycerides, diglycerides, and triglycerides. Oils, which have a
lower melting point than fats, remain liquid in colder temperatures, such as gingelly oil. The cell
membranes are predominantly composed of phospholipids, which contain phosphorus and a
phosphorylated organic compound, like lecithin, and are essential for cellular structure. In certain tissues,
particularly neural tissues, lipids can have more complex structures.
ENZYMES:

Life relies on the coordination of various chemical reactions in living organisms, such as digestion,
absorption of molecules, and energy production. These processes involve a sequence of reactions that occur
under mild conditions, facilitated by biocatalysts called enzymes. Almost all enzymes are globular proteins,
highly specific to particular reactions and substrates. Enzymes are generally named after the compound or
class of compounds they act on. For example, the enzyme that catalyzes the hydrolysis of maltose into
glucose is called maltase. Enzymes can also be named based on the reactions they catalyze, such as
oxidoreductase enzymes, which facilitate the oxidation of one substrate and the simultaneous reduction of
another. The suffix "-ase" is used for enzyme names.

Enzymes are required in small quantities to catalyze reactions. Similar to chemical catalysts, they reduce
the activation energy required for a reaction. For instance, the activation energy for the acid hydrolysis of
sucrose is 6.22 kJ/mol, while it is only 2.15 kJ/mol when catalyzed by the enzyme sucrase. The mechanism
of enzyme action involves this reduction in activation energy, enabling reactions to proceed more
efficiently under mild conditions.
VITAMINS:

Vitamins are organic compounds required in small amounts in our diet to perform specific biological
functions. Their deficiency can lead to specific diseases. While plants can synthesize almost all vitamins,
most cannot be produced by the human body, though some are produced by gut bacteria.

Vitamins are categorized by letters (A, B, C, D, etc.), with some having sub-groups, like B1, B2, B6, B12.

Classification of Vitamins:
1. Fat-Soluble Vitamins: These vitamins are soluble in oils and fats but not in water. They include:
● Vitamin A
● Vitamin D
● Vitamin E
● Vitamin K
These vitamins can be stored in adipose tissue and the liver.
2. Water-Soluble Vitamins: These vitamins are soluble in water but insoluble in fat. They include:
● Vitamin B complex
● Vitamin C

S.No. Vitamin Sources Deficiency Diseases

Carrots, fish liver oil, butter,
(i) Vitamin A milk Xerophthalmia, night blindness
Vitamin B1 Milk, green vegetables, Beriberi (loss of appetite, retarded
(ii) (Thiamine) cereals, yeast growth)
Vitamin B2 Digestive disorders, cheilosis,
(iii) (Riboflavin) Egg white, milk, liver, kidney burning sensation of skin
Vitamin B6 Milk, cereals, egg yolk, grams,
(iv) (Pyridoxine) yeast Convulsions
(v) Vitamin B12 Fish, meat, egg, curd Pernicious anemia
Vitamin C Amla, citrus fruits, green leafy
(vi) (Ascorbic acid) vegetables Scurvy (bleeding gums)
Exposure to sunlight, fish, egg
(vii) Vitamin D yolk Osteomalacia, rickets
Vegetable oils, sunflower oil, Fragility of RBCs, muscular
(viii) Vitamin E wheat germ oil weakness
(ix) Vitamin K Vegetable oils, sunflower oil Increased blood clotting time
NUCLEIC ACIDS:

Nucleic acids, which are the carriers of genetic information, play a crucial role in heredity. They are
composed of two main types: Deoxyribonucleic Acid (DNA) and Ribonucleic Acid (RNA). These
molecules are polynucleotides, long-chain polymers made up of nucleotide units, which consist of a sugar,
a phosphate group, and a nitrogenous base.

Chemical Composition of Nucleic Acids:

Nucleic acids undergo hydrolysis to yield pentose sugars, phosphoric acid, and nitrogenous bases. In DNA,
the sugar is 2-deoxyribose, while in RNA, it is ribose.

DNA contains four nitrogenous bases:

- Adenine (A)
- Guanine (G)
- Cytosine (C)
- Thymine (T)
RNA has four bases as well, with Uracil (U) replacing Thymine (T). The bases in both DNA and RNA are
categorized into purines (A, G) and pyrimidines (C, T, U).

Structure of Nucleic Acids:

Nucleosides are formed by attaching a base to the sugar molecule. Nucleotides are
formed when nucleosides are linked to phosphoric acid at the 5' position of the
sugar. Nucleotides are joined by phosphodiester bonds between the 5' and 3'
carbons of the pentose sugars. Primary and Secondary Structure of Nucleic Acids.

- The primary structure of nucleic acids is the sequence of nucleotides along

the strand.
- The secondary structure refers to the specific folding of these strands. For
DNA, this structure is the double helix, while RNA typically exists in a
single-stranded helix that may fold back on itself.

Functions of Nucleic Acids:

DNA is responsible for the transmission of genetic traits from one generation to
the next. DNA carries the genetic code that is used by RNA to synthesize proteins.
This process involves:
DNA

- mRNA (messenger RNA) carrying the genetic information from DNA to ribosomes.
- rRNA (ribosomal RNA) forming the core of the ribosome structure.
- tRNA (transfer RNA) bringing the appropriate amino acids to the ribosome during protein
synthesis.
HORMONES:

Hormones are chemical messengers produced by endocrine glands that regulate various bodily functions.
They are released into the bloodstream and transported to target cells or organs. Hormones can be steroids,
polypeptides, or amino acid derivatives. They help maintain homeostasis by regulating processes such as
blood glucose levels, stress responses, growth, and sexual development. For instance, insulin and glucagon
control blood sugar, while thyroid hormones regulate metabolism. Steroid hormones like cortisol and
testosterone influence stress responses and sexual characteristics. Hormonal imbalances can lead to
disorders like hypothyroidism or Addison’s disease.
ACKNOWLEDGEMENT:

I would like to take this opportunity to express my gratitude to Mrs. Ritu Goddara, for her encouragement,
guidance and support towards the completion of the project “Amines”.