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Retold by,
Amran Md Said
Matriculation College of Pahang
SUBTOPIC :
1.1 Water
1.2 Carbohydrates
1.3 Lipids
1.4 Protein
1.5 Nucleic acids
1.1 WATER
• The water molecule is electrically neutral but there is a net negative charge on the
oxygen atom and a net positive charge on both hydrogen atoms.
• A molecule carrying such an unequal distribution of electrical charge is called a polar
molecule.
• The positively charged hydrogen atoms of one water molecule are attracted to the
negatively charged oxygen atoms of nearby water molecules by forces called hydrogen
bonds.
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• Hydrogen bonds largely account for the unique properties of water. weaker than
covalent bonds.
• But -> strong enough to hold water molecules together.
• Because of their hydrogen bonds, water molecules are attracted to charged particles or
charged surfaces.
• This means that much energy is needed to turn liquid water into water vapor.
• The amount of heat energy needed to melt ice is very high and the amount of heat that
must be removed from water to turn into ice is also great.
• Many living organism use this feature of water as cooling mechanism.
• For example, human sweat → the liquid water in sweat absorbs heat energy from the
skin or in transpiration from green leaves → to stop the leaves’ temperature from rising
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• Most liquids contract on cooling, reaching their maximum density at their freezing point.
• Water is unusually reaching its maximum density at 4ºC.
• As water freezes, the ice formed is less dense than the cold water around it. The ice
floats on top.
• The floating layer of ice insulates the water below.
• This is why the bulk of ponds, lakes or the sea rarely freeze solid.
• Aquatic life can generally survive a freeze-up.
1.2 CARBOHYDRATES
Learning Outcomes:
Introduction
• Organic molecule containing the element carbon, hydrogen and oxygen in a 1:2:1 ratio
• Written as (CH2O)n ; n = number of carbon
Use of carbohydrates:
• Source of energy
• Storage of energy
• Structural component of cell membranes and cell walls
• Carbohydrates can be classified into three classes:
1. monosaccharides :- single sugars
2. disaccharides :- double sugars
3. polysaccharides :- many sugars
MONOSACCHARIDES
• Physical Characteristic:
1. Small
2. White
3. Sweet
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4. Soluble
5. Can be crystallized
• Chemistry Characteristic
1. reducing Benedict test
2. condensation reaction to form disaccharide or polysaccharide
• Greek words, monos = simple; sacchar = sugar, generally have molecular formula that
are some multiple of CH2O.
• - (CH2O)n For example, glucose has the formula C6H12O6.
• Most names for sugars end in -ose.
• basic unit or monomer
Example :
• Aldehyde group – glyseraldehyde, ribose and glucose
• Ketone group – dihydroxyaceton, ribulose and fructose
Functional Groups
Carbonyl Groups
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If the location of carbonyl group is in the middle backbone of the corbon, it call ketose
Reducing sugar
Benedict’s test
• Benedict’s reagent contains copper (II) ions, which give a blue colour to the Benedict’s
solution.
• When heated with a reducing sugar, the copper (II) ions are reduced to copper (I) ions,
and an orange-red precipitate of copper (I) oxide is formed:
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ISOMER
α and β isomers
At Carbon 1 ,
α glucose – has OH down
β glucose – has OH up
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DISACCHARIDES
• Chemistry characteristic
- Reducing Benedict test (except sucrose)
• A monosaccharide able joined together to form it by a condensation reaction.
• By hydrolysis reaction to form monosaccharide.
Types of Disaccharide
Formation of disaccharide
lactose
• Milk sugar, is found exclusively in milk and is an important energy source for young
mammals
• It can only be digested slowly, so gives a slow steady release of energy.
• Lactose = glucose + galactose
Reducing sugar
All monosaccharides and some disaccharide (maltose and lactose) are type of chemical
reaction knows as reduction.
Sucrose (non reducing sugar) and polysaccharide can’t reducing Benedict test.
POLYSACCHARIDES
• Are formed when many hundreds of monosaccharides condense (join) to form chains.
• The chains formed may be:
- Variable in length
- Branched or unbranched
- Folded – ideal for energy storage
- Straight or coiled
• Characteristic of polysaccharides:
- large,
- not sweet
- Insoluble in water
• Polysaccharides are polymers of hundreds to thousands of monosaccharides joined
by glycosidic linkages.
• Function → is as an energy storage macromolecule that is hydrolyzed as needed.
• Others → serve as building materials for the cell or whole organism.
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STARCH
• Starch is a storage polysaccharide in plants.
• monomers are joined by 1-4 linkages between the α glucose, known as α-1,4 glycosidic
bond .
• unbranched form of starch → amylose → forms a helix.
• Branched forms → amylopectin.
Amylose
• Made from α-glucose molecules
• Forming unbranched helical chain of 300 units in length.
• Each α-glucose is joined by a glycosidic bond between neighbouring C1 and C4 atoms.
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Amylopectin
amylose
amylopectin
Glycogen
Cellulose
• The enzymes that digest starch cannot hydrolyze the beta linkages in cellulose.
• Cellulose in our food passes through the digestive tract and is eliminated in feces as
“insoluble fiber”.
• As it travels through the digestive tract, it abrades the intestinal walls and stimulates
the secretion of mucus.
• Some microbes can digest cellulose to its glucose monomers through the use of
cellulase enzymes.
• Herbivores, like cows , have symbiotic relationships with cellulolytic microbes, allowing
them access to this rich source of energy.
• Cows do have enzymes → amylases, which can break β - 1,4 glicosidic bonds in
starch but which cannot recognize β - 1,4 glicosidic bonds in cellulose,
• the bacteria in the rumen do produce enzymes called cellulles which can recognize
and break β - 1,4 glicosidic bonds in cellulose
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Retold by,
Amran Md Said
Matriculation College of Pahang
1.3 LIPIDS
• General term for any water-insoluble organic molecules that can be extracted from
cells by ethers, benzene, or other nonpolar solvents.
• They contain carbon, hydrogen and oxygen, with far more hydrogen and carbon
compared with oxygen than in carbohydrates;
• They are insoluble in water .
• 3 major classes of lipids
1. triglycerises → e.g. Fat & oil
2. phospholipids → e.g. Lecithin
3. steroids → e.g. Cholesterol & Testosterone
Importance of lipids
• Energy storage
• Component of cell membrane
• Insulation : blubber
• Emulsifiers
• Important carriers or precursors of important flavor and odor compounds.
• Transports fat-soluble vitamins
• Immune system
• Contributes to obesity, coronary heart disease and other health problems.
TRYGLYCERIDE
• Triglycerides with reletively short fatty acid chains, or with unsaturated fatty acids, tend
to be liquid at normal temperaturated and called oils.
• Triglycerides with longer fatty acid chains, or with saturated fatty acid, are more likely
to be solid and are called fats.
• Triglycerides, like all lipids, are insoluble in water. This is because they have no dipoles
and no charges which can attract water molecules.
• Are especially useful as energy stores, because they contain much energy per gram
than either carbohydrates or proteins.
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FATTY ACIDS
Classification of essential
PHOSPHOLIPIDS
STEROIDS
PROTEIN
Protein
• Protein are polymers whose molecules are made from many amino acid molecules
linked together.
• Protein consists of carbon, hydrogen, oxygen and nitrogen.
• Function of protein:
- Enzymatic catalysis .
- Transport of respiratory gases and storage.
- Structure and support
- Contacts or co-ordination (hormones)
- Immunity.
- Growth and development – membrane proteins.
- Heredity
Protein molecule
• Each different proteins molecule is made under the direction of its own gene and
performs its precise function.
• The shape of it is determined by its amino acids sequence.
• Amino acids are the building blocks from which protein are made.
• There are about 20 commonly occuring amino acids in protein.
• All have the same basic structure but differ in their RESIDUAL CHAIN ( R ).
• Amino Acid Structure
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Formation of Polypeptides
Structure of proteins
• A typical protein consists of one or more polypeptide chains which may be folded,
branched and cross-linked at intervals.
• Each proteins has a specific three-dimensional shape.
• In describing the structure of a protein, it is usual to refer to four separate levels of
organization.
• Primary (10), secondary (20), tertiary (30) and quaternary (40) levels of protein.
Primary structure
• This discribe the sequence of amino acids in the protein and usually determines its
eventual shape and biological function.
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Secondary structure
• Once a linear chain of amino acids is formed it spontaneously folds to form α helix or β
pleated sheet.
• Hydrogen bonds holds the secondary structure together.
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Tertiary structure
• Once they have been folded by hydrogen bonds, polypeptides may then fold into a
globular shape which is maintained by
- hydrogen bonds,
- ionic bonds
- disulphide bridge
Example myoglobin.
Quaternary structure
• Consists of more than one polypeptide chains to form a single functional molecule
• Held together by hydrophobic interactions, hydrogen bonds, ionic bonds and disulfide
bridges
• Associated with non-protein groups into a large complex protein molecule
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• It consists of four chains (two α-polypeptide chains and two β-polypeptide chains)
wrapped around an iron hem group.
• Structure of protein maintain by hydrogen bond ( 2 , 3 and 4); ionic bond, hydrophobic
interaction, disulfide bridge and van de waals interaction ( 3, 4)
• Breakage the bond causes loss of specific three-dimensional shape of a protein
molecule
• They change may be temporary or permanent
• Example: Proteins are easily damaged by heat (temperatures greater than 40 0C) due
to breakage of their cross linkages
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• This cause the protein molecules to open up, straighten the folds and assume a
random configuration
• For some proteins, denaturation might be reserved when normal conditions are
restored
• Classifation base on structure
• Divided by 3 classification base on structure.
- Conjugated protein
- Globular protein
- Fibrous protein
Conjugated Protein
Globular Protein
Fibrous Protein
Properties of protein
• Amphoteric
• Buffering capacity
• Colloidal properties
• Denaturation
Note :
Properties of Protein, just for extra knowledge
Properties of protein
1. Amphoteric
• In aqueous as neutral (pH 7), amino acid such as dipole, its called zwitterions
• Amphoteric because have characteristic both acidic and basic.
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• In aqueous acidic (< pH 7), protein receive H+ and make its positive charge.
• In aqueous alkaline (>pH 7), donate H+ and make its negative charge.
• Charge at zwitterions depend on pH
• pH at amino acid as neutral like electric its call isoelectric
• All amino acids have own characteristic as isoelectric point (pI).
2. Buffering capacity
3. Colloidal properties
4. Denaturation
• The structure of a protein can be change if the bonds which hold it in shape are
broken. This process is called Denaturation.
• High temperatures break hydrogen bond and van der Waals forces. In a globular
protein a long chain instead of a curled-up ball. The molecules will no longer be soluble
in water.
• Extremes of pH break ionic bond, because they alter the charges on R groups.
• Reducing agents break disulphide bond. This is made use of when perming hair.
Keratin, from which hair is made, contains disulphide bond that hold the shape in
shape.
NUCLEIC ACID
Topic distinguish
• Describe the structure of nucleotide as the basic composition of nucleic acid (DNA and
RNA)
• Describe the structure of DNA based on the Watson and Crick Model.
• State the type and function of RNA
• State the differences of DNA and RNA
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Nucleic acids
• The amino acid sequence of a polypeptide is programmed by a gene.
• A gene consists of regions of DNA, a polymer of nucleic acids.
• DNA (and their genes) is passed by the mechanisms of inheritance.
Structure of nucleotide
Phosphate group
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Pentose sugar
Nitrogenous base
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DNA
• James Watson and Francis Crick postulated double helix of 2 nucleotides strands
• Nucleotide strands being linked together by pairs of nitrogenous bases which are
joined by hydrogen bonds
• Purines ; double ring structures form longer links if paired together than pyrimidide
• Only by pairing 1 purine with 1 pyrimidine – consistent separation of 3 rings’ width can
be achieved
• Deoxyribose and phosphate units form the uprights while nitrogenous base pairings
form the rungs
• 2 chains that form the uprights run in opposite direction (antiparallel)
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RNA
rRNA
• Large,complex molecule
• Made up of double and single helix
• Manufactured by DNA of the nucleus
• Found in ribosome
• Comprises of more than half the mass of the total RNA of the cell
• The Base sequence is similar in all organisms
tRNA
mRNA
Amran Md Said
Matriculation College of Pahang
– The End -