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Biological Molecules
Biological Molecules
2: Biological molecule
Biological molecules are any molecules that occur Objectives of the chapter 5
By the end of this chapter students should be able:
naturally in living organisms.
▪ to use and understand the terms macromolecule and polymer
- The branch of biology which study of biological ▪ to describe the importance of and basic structure of carbohydrates
molecules known as molecular biology (monosaccharides, disaccharides and polysaccharides)
Biological molecules can either organic (its main element ▪ to describe the formation and breaking of a glycosidic bond by
is carbon (C) e.g. Carbohydrate, proteins lipids and condensation and hydrolysis respectively
nucleic acids) Or in-organic molecules (mainly don’t ▪ to relate the structures of the polysaccharides; starch, glycogen and
contain carbon such as water). cellulose to their functions in living organisms
▪ to describe the structure and formation of the most common type of lipid,
❑ Macromolecule and polymer: the triglyceride.
▪ to relate the structures of triglycerides and phospholipids to their
Large organic biological molecules are called functions in living things
macromolecules (there are four macromolecules ▪ to use and understand the terms hydrophobic and hydrophilic,
carbohydrates, proteins, nucleic acids, and lipids.) unsaturated and polysaturated as they apply to lipids.
Polymers are macromolecules that made up of many repeating subunits that are similar or identical to each other.
(Carbohydrates, proteins, and nucleic acids are all polymers because they are made up of many identical repeating subunits.)
The small organic molecules (subunits) joins to form polymer is known as monomers. E.g. monosaccharides, amino acids
and nucleotides.
❑ Carbohydrates:
Carbohydrates are biological molecule contain the elements carbon, hydrogen and oxygen.
- The ‘hydrate’ part of the name comes from the fact that hydrogen and oxygen atoms are present in the ratio of 2:1, as
they are in water (‘hydrate’ refers to water).
The general formula for a carbohydrate can therefore be written as Cx(H2O)y. ✓ The term “saccharide” derives
There are three types of carbohydrates: from the greek word “sakcharon”,
1. Monosaccharide (Glucose, Galactose and fructose) which means sugar.
2. Disaccharide (maltose, sucrose and lactose)
3. Polysaccharide(starch, glycogen and cellulose)
The main functions of carbohydrate are:
▪ They are an immediate source of energy (glucose).
▪ They provide shape to certain cells (cellulose and chitin in plant and fungi cell walls respectively)
▪ They are the components of mucus, some hormones, many antibiotics, and coenzymes.
▪ They are an essential part of the nucleic acids, DNA and RNA.
▪ They also are components of cell membranes.
Monosaccharides:
Monosaccharides (also known as simple sugars) are simplest forms of carbohydrates. Its basic subunits (monomers) that
make up complex carbohydrates which are polymers.
- Properties of monosaccharides usually are sweet, soluble in water and colorless.
Monosaccharides have general formula (CH2O) n. where n represents number of carbon atoms and are small integer
(3 up to 10).
One important aspect of the structure of pentoses and hexoses is that the
chain of carbon atoms is long enough to close up on itself and form a more
stable ring structure.
The hydroxyl group, –OH, on carbon atom 1 may be above or below the plane of
the ring. If the form of glucose where it is below; the ring is known as α -glucose
(alpha-glucose) and the form where it is above the ring is β -glucose (beta-glucose)
Disaccharides:
Disaccharides (double sugars) are composed two monosaccharides joining together. The three most common disaccharides are:
1. Maltose – malt sugar (glucose + glucose): products of digestion of starch.
2. Sucrose - table sugar (glucose + fructose) : found in fruits
3. Lactose – milk sugar (glucose + galactose): found in milk. (All they have same molecular formula “C12H22O11”)
The process or chemical reaction joining of two monosaccharides to form disaccharide known as condensation reaction.
During this reaction; one molecule of water is released and the bond forms between two monosaccharides is called glycosidic
bond. This bond is between carbon atom 1 of one monosaccharide and carbon atom 4 of the other, it’s known as a 1, 4 glycosidic
bond.
When water is added disaccharides break down into its monosaccharides; this reaction known as hydrolysis (its reverse of
condensation). This takes place during the digestion of disaccharides when they are broken down to monosaccharides.
❑ Lipids:
Lipids are a diverse group of biological molecules. Lipids are insoluble in water
because they are non-polar. Just like carbohydrates, lipids are mainly composed of
carbon, hydrogen, and oxygen. But Lipids generally have very small amounts of
oxygen, compared with the amounts of carbon and hydrogen.
Steroids:
Steroids are another group of lipid molecule which
composed four fused rings.
Common steroids include; cholesterol (found in
cell membranes and helps maintains it fluidity and
also necessary for the manufacture of vitamin D),
testosterone, progesterone and ecdysone (molting
hormone of insects).
High cholesterol levels can lead to clogged arteries that come from a process known as atherosclerosis.
Functions of steroids:
▪ It helps metabolisms such as making Vitamin D.
▪ It also controls the development sexual characteristics.
Testing for lipids:
One of the testing for lipids is known as emulsion test. Ethanol is added to the unknown substance and mixture is gently
shaken. This allows any lipids in the substance to dissolve in the ethanol. The ethanol is then poured into a tube containing water.
If lipid is present, a cloudy white suspension forms and this kind of mixture is called an emulsion.
By the end of this lesson, students should be able:
❑ Proteins: ▪ to describe the basic structure of amino acids, the
Proteins are polymers that consist of amino acid chains. More than 50% of basic component of proteins.
the dry mass of most cells is proteins. ▪ to describe the formation and importance of the
Proteins have many important functions include: peptide bond.
▪ all enzymes are proteins ▪ to describe the primary structure of
polypeptides and proteins and how it affects their
▪ proteins are essential components of cell membranes
secondary and tertiary structure
▪ some hormones are proteins – for example, insulin and glucagon ▪ to describe the importance of hydrogen bonds,
▪ the oxygen-carrying pigments haemoglobin and myoglobin are proteins disulphide bonds, ionic bonds and hydrophobic
▪ antibodies are proteins which attack and destroy invading microorganisms. interactions in maintaining the three-dimensional
▪ collagen, another protein, adds strength to many animal tissues, such as structure of proteins
bone and the walls of arteries ▪ to describe how the structures of globular (e.g.
▪ hair, nails and the surface layers of skin contain the protein keratin haemoglobin) and fibrous (e.g. collagen) proteins
▪ actin and myosin are the proteins responsible for muscle contraction. are related to their functions
▪ proteins may be storage products – for example, casein in milk and albumin in eggs.
Amino acids:
Amino acids are the basic structural units of proteins. They all have a
central carbon atom which is bonded to an amine group, –NH2 , and a
carboxylic acid group, –COOH. It is these two groups which give amino
acids their name. The third component that is always bonded to the carbon
atom is a hydrogen atom. The only component in which amino acids differ
from each other is in the remaining, fourth, group of atoms bonded to the
central carbon. This is called the R group.
Protein structure:
Proteins can be classified biologically into four levels of structures:
Primary structure Primary structure of protein is a sequence of amino acids a polypeptide chain. Its linear chain because
only has peptide bonds between amino acids.
Secondary structure Secondary structure of protein is most basic level of protein folding. The secondary structures are a
polypeptide chain which coiled into α-helix or folded into β-pleated sheet. It folded or coiled chain
because the hydrogen bond between amino acids in polypeptides and this numerous hydrogen bond makes
a secondary structure stable.
This secondary structure is due to hydrogen bonding forms between the oxygen of the –CO– group of
one amino acid and the hydrogen of the –NH– group of another amino acid within a single polypeptide.
Tertiary structure When the secondary structure itself is coiled or folded forms three-dimensional folding known as
tertiary structure.
Every protein has a unique tertiary structure
which is responsible for its properties.
This is the result of four possible types of bond
folded proteins in their precise shapes and they are:
▪ Hydrogen bonds can form between a wide variety of R groups.
▪ Disulfide bonds form between two cysteine molecules, which contain sulfur atoms.
▪ Ionic bonds form between R groups containing amine and carboxyl groups.
▪ Hydrophobic interactions occur between R groups which are non-polar, or hydrophobic.
Quaternary structure This structure is found only complex proteins that contain more than one polypeptide chains and also non-
protein groups associated with the molecules.
❑ In-organic ions:
Living organism also needs in-organic ions which take important part metabolic reactions in the body. The table below shows
inorganic ion and their main functions:
Calcium ions Ca2+ In animals; necessary for: formation of bones, contraction of muscles and blood clotting. In
plants; its major component of middle lamella of the cell wall and also aids for translocation of
carbohydrates and amino acids.
Sodium ion Na + Its important for transmission of nerve impulses, maintains osmotic pressure of the body fluids
and helps reabsorption of water in kidneys. Also its constituent of sap vacuole in plant and so
helps to maintains turgidity.
Potassium ion K + It is important for transmission of nerve impulses, its acts as cofactor of enzymes in
photosynthesis and respiration and its responsible for turgidity of guard cells and controls
opening and closing of stomata.
2+
Magnesium ion Mg It is an important for making chlorophyll and acts as cofactor which activates ATPase. Also its
necessary for formation of bones.
Chloride ionCl - It is important for transmission of nerve impulses and such like sodium ion also help reabsorbs
of water in kidney. Also needs for formation of hydrochloric acids in gastric juice.
3-
Nitrate ion NO Its important for making amino acids, vitamins, nucleotides, coenzymes and ATP. Also some
hormones contain nitrogen.
Phosphate ion PO43- Are important components of ATP, nucleotides and some proteins. also are components of bone.
Iron ion Fe2+ Its necessary for formation of heamoglobin in erythrocytes.
-
Iodide ion I Its necessary for formation of thyroid hormones.