Name: Lim Soong Xian

Class: 6RS1/6AS1
No Title Remark
Biological Molecules
Organic Inorganic
- Contains carbon - Does not contains carbon
- Produced by living cell - Cant be produce by living cell
- Example: Lipids - Example: Water

1.1 Water
Chemical Properties/Characteristics of Water
Bond angle (104.5 )
Polar molecule: Oxygen atom is slightly negative; hydrogen
atoms are slightly positive.
Universal solvent: Including ionic compound like salt (sodium
chloride, NaCl) but is also a suspension which is a mixture of
liquids with particles of a solid which may not dissolve in the liquid.
Covalent bond between hydrogen (H) and oxygen (O)
Hydrogen bonds
Weak pH sensitive Temperature sensitive
A large amount of hydrogen bonds forming H2O molecules so a lot of energy is needed to
break it down.
Hydrogen bond in between H2O hold in close together (break and reform at high
frequency)
Water ensure body temperature not fluctuate (not increase too high or too low) so enzyme
works perfectly

Physical Properties/Characteristics of Water

High specific heat capacity - (4.2kJ/ kg/ C) A lot of heat energy is needed to make a
slight increase in water temperature
High latent heat of vaporization - (2260J/kg) A lot of heat energy is needed to change
water from liquid to gas form to overcome hydrogen bond between H2O molecule
[sweating (human), panting (dog), transpiration (plants)] [cooling effect] these enable
them to loss a large amount of heat BUT with minimal loss of water
High cohesion force- as high attractive force between H2O molecules because of
hydrogen bond between H2O molecules.
 High adhesion force- (is the attraction between H2O & other substance) as this enable
water transporting in the plant (xylem) for transpirational pull as adhesion>gravity. A
narrow xylem vessel is better for capillary action to form continuous water column
(unbreakable)
High surface tension results from collective strength from hydrogen bond (and have a
thin invisible film)
Ice is less dense than water (max density= 4C) as this prevent the water from freezing
during winter as it insulates the layer below from further cooling and freezing (during
winter)

Water Ice
Occupied less space Occupied more space
Compact Spacious

1.2 Carbohydrates
Organic compound Polymer- Macromolecule made out of monomer
C, H, O (element) with the ratio 1:2:1 Monomer- Repetition same basic unit
Sugar-containing compound
Most common organic compound is plant with cellulose
Many C-H bonds
General formula Cx(H2O)y: Example: Glucose (C6H12O6), [Sucrose (C12H22O11) cause
condensation of H2O]
Provides energy
Source of energy for cell as respiratory substrate (Example: Glucose)
Energy storage: [Human, animal (glycogen)] [Plants (starch)]
Divided into 3 classes: monosaccharide (simple sugar); disaccharide (double sugar);
polysaccharide (complex basic unit)
Monosaccharide
Physical Properties
Sweet
Dissolve in water (affect osmotic concentration [])
Form white crystals
Polar molecule (-OH readily form hydrogen)
Bond in water
Chemical Properties
Functional group
Aldehyde group Keto group
-CHO -C=O

Aldoses Ketoses
Example: Glucose Example: Fructose

All are reducing sugar (carry out reduction when react with Benedict solution) [Reduce
CuSO4 to Cu2O
CuSO4 Cu2O
Blue Brick-red precipitate
Cu Cu
Soluble Insoluble
 Glucose ring structure

Physiological Roles
Respire by cells to release energy
Balance water potential within cell and in blood
Forms polysaccharide
Aldose (-CHO) Ketose (C=O)
Triose (3c) glyceraldehyde Dihydroxyacetone
Tetroses (4c) Intermediary product during Intermediary product during
glycosis glycosis
Pentoses (5c) - Ribose - Ribulose [Receptor for
- Dixoyribose fixation of CO2 (Calvin cycle)
Hexoses (6c) - Glucose - Fructose
- Galactose
 Triose (3c)

Pentoses (5c)

Hexoses (6c)
Disaccharides
Monosaccharide + Monosaccharide (hydrolysis) Disaccharide
Disaccharide (condensation) Monosaccharide + Monosaccharide
Physical Properties
Soluble
Sweet
Crystalised form
Examples: Sucrose, Maltose, Lactose
Chemical Properties
Reducing sugar (except sucrose)
Sucrose does not have free functional group to carry out reduction.
Can be hydrolised into monosaccharide by dilute acid (heated) using specific enzyme
Double sugar: Bonding between monosaccharide
Glycosidic bond
Maltose ( glucose + glucose) 1,4 glycosidic-bond

Lactose ( glucose + galactose) 1,4 glycosidic-bond

Sucrose ( glucose + fructose) 1,2 glycosidic-bond

Lactose
Polysaccharides
- Complex carbohydrate/ sugar
- Biopolymer
- (C6H10O5) n
- Examples: starch, glycogen cellulose, chitin, murein (peptidoglycan), fibre (insulin),
oligosaccharide (3-14, monomer)
Chemical Properties
- No reducing power
- Easily hydrolysed
- Starch + Glycogen (hydrolysed by amylase) maltose -glucose
- Cellulose (hydrolysed by cellulose) -glucose (created by microbes and snails)
Physical Properties
- White powder (extracted)
- Dissolve in hot water and become colloidal sol (got suspension, not really dissolved)
- Colloidal sol become gel when dried up
- Insoluble
- Not sweet
- Cannot be crystalised
- Compact and osmotically inactive (Osmotic concentration will not be affected)

Starch
- Amylose at centre (15%-20%)
- Amylopectin at periphrases (80%-85%)
- glucose (monomer)
- 1,4 glycosidic-bond
- 1,6 glycosidic-bond
Amylose
- Straight Chain
- Unbranched
- - helix coil (hydrogen, H bonds among CH2OH group (1 coil: 6 - glucose)
- Soluble in hot water without forming starch gel
Amylopectin
- Straight chain
- Branched
- - helix coil

Glycogen
- Animal starch
- Monomer ( glucose)
- Looks like amylopectin but larger
- Extensively branched
- White powder form
- 1,4 glycosidic-bond
- 1,6 glycosidic-bond
Physiological role
- Store energy for animal and fungi
- Store in liver and muscle cell
- Regulate blood glucose level
Cellulose
- Monomer ( glucose)
- 1,4 glycosidic bond
Structure
- Microfibril pattern
- Branched
- No coil
- Straight
- Each glucose related to next by a rotation of 180
- CH2OH group found alternatively up and down the plane
- Crossed link by hydrogen bond

Physiological role
- Converted into free glucose by the liver
- Herbivore (cow, horse termite) utilise it with the help of bacteria living in guts to digest it
- Food source for bacteria, fungi and protozoa
- Form cell wall for protection and support in plants
1.3 Lipids
Physical Properties
- Little O2 so it tends to be hydrophobic (not soluble in water)
- Soluble in non-polar organic solvent (chloroform, acetone, ether, benzene)
- Lower density than water
- High viscosity (liquid's resistance to flow)
- Greasy
Chemical properties
- Made up of hydrogen, carbon, oxygen
- Contains higher proportion of CH2 (hydrocarbon)
- It is not soluble in water as all H atoms bonded to C atoms, there is no tendency to form
hydrogen bond with H2O
- Esters formed from fatty acid and alcohol
- Examples: triglycerides (fats), phospholipid, steroids, waxes and terpenes.

Triglyceride (Triacylglycerol)
- Formed from 1 molecule of glycerol (alcohol group) and 3 molecules of fatty acid
(carboxylic group) through the process called esterification.
- Esterification is condensation between an alcohol group and a carboxylic group.
- Esterification is also called lipogenesis that is one molecule of glycerol react with three
molecules of fatty acid

Physical Properties
- Insoluble in water
- Float on water as it has lower specific gravity than water (waterproof layer of water)
- Soluble in non-polar organic solvents like acetone
- Form emulsion if shaken with alcohol
- Leave behind grease spot on paper
Chemical Properties
- Compact
- React with atmospheric oxygen and become rancid when kept for too long
- React with Sudan lll reagent to form dark red complex.
- Hydrolysed by lipase or boiling with dilute alkali to form glycerol and fatty acid
Physiological Roles
- Heat insulator layer to keep body warm
- Long term energy store
- For animals, it is stored as oil droplet in the cytoplasm of the adipose cells
- Adipose cells are found underneath the skin, in the mesentery or surrounding the intestines,
kidney and the heart which is found between muscle fibre
- In plants, they are found in seeds and fruit walls (oil palm fruits, raspberry, sunflower seeds
and kernel of cereals.
Saturated fats - Contains only single bond with double covalent bond between carbon
CH2CH2CH2 atoms
- Solidify when cooked
- Not readily metabolised (compared to unsaturated fats)
- Readily deposited on inner layer (cholesterol)
- Examples: Animal fats, coconut oil
Unsaturated fats - Contains at least one double covalent bond
CH2CHCHCH2 - Readily metabolised
- Not readily solidify when cooked
- Polysaturated fatty acid
- Essential fatty acid
- Examples: Plant oil
Phospholipids
(1 glycerol + 2 fatty acid + 1 phosphate acid)
Physical Properties
- Hydrophilic head is polar (soluble in water) cause forming spherical micelle
- Hydrophobic tail is non-polar (insoluble in water)
- Amphipathic properties (having both hydrophilic and hydrophobic parts)
- Example: Lecithin (extract form soy)
Structure

Distribution
- Found in all plasma membrane
- Found in organelles membrane in cell
Function
- Enable neurone to synthesis acetylcholine (a type of neurotransmitter for muscle contraction)
- Enable cell membrane to be semi permeable
- Main component of cell membrane and organelle membrane by forming phospholipid bilayer
- Transporting fat to the body
Steroid
- Saturated fats (animal)
- Examples: Cholesterol, sex hormone
Function
- Insoluble in water
- Example: Cholesterol/ Progesterone/ Testosterone
Structure
- 4 fused carbon rings- 3 hexagon and 1 pentagon

Cholesterol
- Synthesised in the liver.
- Used to synthesise vitamin D in the skin.
- Excess cholesterol in the body can lead to arteriosclerosis, high blood pressure and heart
attacks.

-
Amino Acids
- Organic compound consisting of carbon, hydrogen, oxygen, nitrogen and sometimes
sulphur and phosphorus.
- Natural polymer, the monomer of protein is amino acid
- Sensitive to heat
- Not soluble
- Amphoteric: shows both acid and base properties
- There are 20 types, smallest is glycine
Polar
- Polar amino acids are amino acids with a polar side group.

Non-polar
- Non-polar amino acids are amino acids with a non-polar side chain
Basic Amino Acid
- Basic amino acids have side chain which is an amino group, NH2, a base group

Acidic Amino Acid

- Acidic amino acids have a side chain which is a carboxylic group, COOH.

Polymerisation of Amino Acid

- H2O removed forming peptide
bond through condensation from
joining carboxyl group of amino
acid and amino group to catalyzed
by enzyme.
Structure
- Up to 20 types of amino acids.
- Linked together by peptide bond
Properties
- Amphoteric
- Its structure has basic and acidic group.
- Amino group, NH2 is basic; while carboxyl group, COOH is acidic.

- pH buffer
- The amphoteric nature of protein allows it to function as a buffer.
- Amino groups of proteins remove excess acids in the system.
- Carboxyl groups neutralise the excess bases in the system.

- Colloidal nature
- Colloids are particles not soluble in water but remain suspended in the solution.
- Most globular proteins are soluble in water due to the small size of its molecule and
existing polar groups such as -COOH.
- Globular protein with larger molecules will from colloidal suspensions in water.
 - Examples: Milk, Gelatin, Starch
Protein denaturation.
- Change of structure and shape of the protein molecule due to the breaking down one or
more bonds maintaining the structure of protein molecule is called protein denaturation.
- Caused by acids, bases, heat, pH and ultraviolet light.
Level of protein structure
- Primary structure
- Primary structure is structure showing the number and sequence of amino acids in its
molecule.
- Linear sequence of amino acid by joining amino acid with peptide bond to form
polypeptide bond
- Determined by specific genetic code found in DNA

- Secondary Structure
- Showing the coiling of polypeptides to become helix or the folding of polypeptide to
become pleated-sheet.
- Maintained and stabilised by hydrogen bonds
- Arranged and parallel to each other
- Tertiary Structure
- Specific coiled and folded of secondary structure
- Form compact globular shape
- Maintained by hydrogen bond, ionic bond, disulphide bridge, hydrophobic interception
and Van der Waals force
- When protein coiled, it shields hydrophobic side groups and only expose hydrophobic
side chain, so protein become soluble

- Quaternary Structure
- Consist of more than 1 subunits of globular protein (become a larger protein)
- Separated tertiary structure and held together by hydrogen bond, ionic bond and
hydrophobic interaction
Composition and structures of protein
1. Proteins can be classified according to its composition or structure.
2. Based on composition, proteins can be grouped into:
simple protein
conjugated protein
3. Based on structure, proteins can be divided into:
Fibrous protein
globular protein

Simple protein
Proteins that contain amino acids only.
For examples: albumin, globulin, and histone.

Conjugated protein
Protein bounds to non-protein groups.
Non-protein groups which bound to proteins are known as prosthetic groups.
For example: haemoglobin.
 Structure of haemoglobin

Fibrous protein
(a) Fibrous protein consists of long and parallel polypeptide chains.
(b) The polypeptide chain in fibrous protein is usually coiled to form -helix.
(c) Neighbouring helical chains are usually cross-linked by hydrogen bonds, electrovalent bonds,
or disulphide bonds.
(d) Fibrous protein are not soluble in water and are very strong.
(e) Examples of fibrous protein:

Collagen - in tendons, cartilages, bones and skin.

Myosin - structural protein in muscles.
Keratin - structural protein in hairs, nails, feathers and horns.
Elastin - found in ligaments.
Sclerotin - combines with chitin to form the exoskeleton of insects.
(f) Collagen is the most common protein in mammals.

This protein is a main structural component of connective tissues (cartilage, skin, tendons
and ligaments).
The basic structure of collagen is a tropocollagen helix which consists of three
polypeptide chains (helixes) twisted together.
The chains are stabilised by hydrogen bonds between the protein chains.
 Collagen fiber

Globular proteins
(a) In globular proteins, the polypeptides (helixes) are folded into globular structures.
(b) The globular structure is maintained and stabilised by hydrogen bonds, disulphide bonds and
electrovalent bonds.
(c) Some globular proteins are soluble in water; some of them form suspension, and the rest are
insoluble in water.
(d) Globular proteins are easily denatured. This is because the hydrogen bonds and disulphide
bond in the molecule can easily be broken.

Denaturation of protein
(e) Examples

Haemoglobin

Myoglobin
Hormones
Enzymes