BIOLOGICAL

MOLECULER
By. Yasmine Hadiastriani
 CARBOHYDRATE
 Consists of molecules : Carbon (C), Hydrogen (H),
and Oxygen (O).
 Most of carbohydrate are large – consists of
complex molecules composed of long chains of
monosaccharide
 Single monosaccharide are also called
carbohydrate
 Divided into :
1. Monosaccharide
2. Disaccharide
3. Polysaccharide
 MONOSACCHARIDE
 The simplest carbohydrate
 These are sugars
 Divided into : Glucose, Fructose, and Galactose
 Usually called as hexose sugars – each monosaccharide has
six carbon atoms in each molecules
 Molecular formula is C6H12O6 in the form of linear
molecules or a ring made up of carbon atoms and one
oxygen atom
 Monosaccharide, especially glucose has two forms – alpha
(α) and beta (β), differ in the location of the OH group on
the number 1 carbon atom
 Glucose’s structure is related to its function
 Its structure makes it soluble so it can be easily
transported. Its chemical bonds contain lots of energy
α-glucose and β-glucose molecules

The two types of

glucose have
these groups
reverse

DonKey : beta-glucose has the H on the

bottom at the structural diagram
 DISACCHARIDE
 Made from two monosaccharides link
together by glycosidic bonds in a
condensation reaction
 Condensation – bonding of a hydrogen (H)
on one monosaccharide to a hydroxyl (OH)
group to produce Glycosidic Bond and
releasing a molecule of water
 Disaccharide can be split apart into two
monosaccharides by hydrolysis reaction
 Hydrolysis – breaking the glycosidic bond by
adding a molecule of water in the reaction
 GLYCOSIDIC BONDS
 Bonding two monosaccharides on the oxygen molecules to
produce disaccharide
 Can form in different places in different molecules
 Six carbon atoms bond in the rings of glucose are numbered
1 to 6. E.g. Maltose – the glycosidic bonds between carbon 1
on α-glucose and carbon 4 of the α-glucose, so it’s a 1-4
glycosidic bond

Disaccharide Monosaccharide Glycosidic Bond

 Glicosidic Bond of Disaccharide :
Lactose β-glucose + galactose 1-4
Sucrose α-glucose + fructose 1-2
CONDENSATION AND HYDROLYSIS
TWO α-GLUCOSE MOLECULES ARE JOINED TOGETHER BY A
GLYCOSIDIC BOND TO FORM MALTOSE

H
HH

Hydrolysis

H2o is
removed
SATURATED AND UNSATURATED LIPID
 The difference is the HYDROCARBON TAILS of the
FATTY ACIDS
SATURATED UNSATURATED
Mainly found in animal fats (e.g. Mostly found in plants (e.g. olive oil)
butter)
Melt at high temperatures Melt at lower temperatures than
saturated ones
Don’t have any double bonds Have double bonds between carbon
between their carbon atoms – atoms, which cause the chain to kink
every carbon is attached to at least
two Hydrogen atoms
TRIGLYCERIDE AS THE ENERGY
STORAGE MOLECULES
1.Long hydrocarbon tails of the
fatty acids contain lots of
chemical energy – a load of
energy is released when they’re
broken down. It also makes lipid
contain twice as much energy
per gram as carbohydrate
2.Insoluble. Triglyceride bundle
together as insoluble droplets in
cells because the fatty acid tails
are hydrophobic – the tails face
inward, shielding themselves
from water with their glycerol
heads
 PROTEIN
 Made from long chains of Amino Acids
 Two Amino acids join together will form a
dipeptide
 More than two amino acids join together
will form a polypeptide
 Proteins are made from one or more
polypeptide
 Protein’s primary structure determines its
3D structure
 AMINO ACIDS
 Molecules that consists of a carboxyl group (-COOH)
and an amino group (-NH2) attached to a carbon
atom
 The difference between different amino acids is the
variable group (R on diagram) they contain.
 PEPTIDE BONDS
 Bonding to link the amino
acids to form dipeptides
and polypeptides.
 It’s a condensation
reaction, so it release
water during the reaction.
 The reverse action is by
adds the water molecule
to break the peptide bond
– Hydrolysis reaction
 Condensation reactions
also called as ‘Synthesis’
reactions
 PROTEIN FOUR STRUCTURAL LEVELS
1. PRIMARY STRUCTURE – sequence of amino acids in
the polypeptide chain
2. SECONDARY STRUCTURE – coiled structure of the
amino acid because of the Hydrogen bonds between
the amino acids in the chain and make the chain
fold into α (alpha) helix and β (beta) pleated
structure
3. TERTIARY STRUCTURE – the coiled or folded of
amino acid chain. For proteins made from a single
polypeptide chain, the tertiary structure forms their
final 3D structure.
4. QUATERNARY STRUCTURE – Several different
polypeptide chains that held together by bonds. It’s
the way to assemble the polypeptide. e.g.
Haemoglobin is made from four polypeptide chains.
For proteins made from more than one polypeptide
chain, the quaternary structure is the protein’s final
3D structure
TYPE OF BONDS RELATE TO STRUCTURE
1. PRIMARY STRUCTURE – peptide bonds
2. SECONDARY STRUCTURE – hydrogen bonds, create α-helix chains
or β (beta)-pleated sheets
3. TERTIARY STRUCTURE – affected by few kind of bonds :
 Ionic interaction : weak attraction between negative and positive
ion charges on different parts of the molecule
 Disulphide bonds : bonds between two sulfur atom of two cysteine
amino acid when they are come close together.
 Hydrophobic and hydrophilic interaction : when the hydrophobic
group close together in the protein, they tend to clump together and
make the hydrophilic group to be pushed to the outside, and affect
protein folds up into its final structure
 Hydrogen bonds : weak bonds between a positive and negative
hydrogen atom between two molecules.
4. QUATERNARY STRUCTURE – determined by the tertiary structure
of the polypeptide, so it can be influenced by all the bonds
 SPECIAL CHARACTER OF PROTEIN
 Protein’s primary structure determines its 3D
structure – the amino acid sequence determines
what bonds will form and how protein will fold up into
its 3D structure. E.g. if there are many cysteines,
these will form disulfide bonds and the protein folds
up in a certain way
 Protein 3D structure is related to the function – e.g.
Insulin’s function is to make cell take up glucose from
the blood. Insulin is a compact protein, which is makes
it easy to transport around the body in the blood
GLOBULAR AND FIBROUS PROTEIN
GLOBULAR PROTEIN FIBROUS PROTEIN
Round, compact, and made Long, insoluble polypeptide
from multiple polypeptide chains, tightly coiled round
chains each other and form rope
shape
The chains are coiled up so The chains are held together
the hydrophilic parts of chain by lots of bonds (e.g.
are on the outside of the disulphide and hydrogen
molecule and the hydrophobic bonds), which make the
parts of chains face inwards protein strong
Soluble – easily transported in Fibrous protein are often
fluids found in supportive tissue
e.g. haemoglobin e.g. collagen
 EXAMPLE OF PROTEIN BASED
ON THE FUNCTION
A. HAEMOGLOBIN
B. ENZYME
C. ANTIBODIES
D. TRANSPORT PROTEINS in CELL MEMBRANES
E. STRUCTURAL PROTEINS, E.G. COLLAGEN
 HAEMOGLOBIN
 Has roughly spherical 3D shape
 Made of four polypeptide chains (2 α-
polypeptide and 2 β-polypeptide),
each polypeptide consist of 1 Haem
group
 Soluble – easily to be transported in
blood. The four polypeptide chains are
coiled up so the R groups (hydrophilic)
are on the outside of the molecules
and they form the hydrogen bonds
with water molecules. The
hydrophobic R groups are inside the
molecule
 The Haem group contained within the
polypeptide has the ion Fe2+ so they
can bind with the Oxygen molecule (2
oxygen atoms). One haemoglobin
molecule can combine with four oxygen
molecule (8 oxygen atoms)
 COLLAGEN
 Strong, fibrous protein that form supportive tissue in
animal.
 High Tensile Strength and compact - Made of three
polypeptide chains that tightly coiled into triple helix
which interlinked by strong hydrogen bonds.
 Minerals can bind to the triple helix to increase its
rigidity
 Insoluble – collagen molecules are very long and too large
to be dissolved in water
 Form the fibers
WATER FUNCTION :
1. Reactant – loads of important chemical
reactions. E.g. photosynthesis and hydrolysis
reaction
2. Solvent – some substances dissolved in it
3. Transport substance – water is liquid and
solvent, so it is easily to transport all materials,
e.g. glucose and oxygen
4. Homeostatic – control temperature by away heat
energy when it evaporates and cools the surface to
decrease temperature
 WATER STRUCTURE
 Water (H2O) consists of two Hydrogen atoms and one
atom Oxygen by shared electrons
 The negative Hydrogen electron pulled towards the
oxygen atom, and the other side of each hydrogen
atom is left with a slight positive charge
 The unshared negative electrons on the oxygen atom
give it a slight negative charge
 This makes water a polar molecule – it has a negative
charge on one side and a positive charge on the
other side.
 The negative charged oxygen atoms of water attract
the positive charge hydrogen atoms – hydrogen
bonding
WATER POLARITY
 Water molecules are very cohesive – very attract
with another water molecules, it helps water to
flow and transport substances
 Water has the negative and positive end and they
can bind with the negative or positive ion. Water
will surround the ions – dissolved
 Water polarity makes it useful as a solvent
HYDROGEN BONDS OF WATER
 The hydrogen bonds between water
molecules can absorb a lot of energy
 Water has a high specific heat capacity – it
takes a lot of energy to heat it up
 Water can stop rapid temperature changes
and allow their temperature stable
 It takes a lot of energy to break the
hydrogen bonds between water molecules,
because water has a high latent heat of
evaporation
 It means that water great for cooling things