Topic: Lipids and Amino

Acid
 
Sub Topic: Carbohydrate
and Nucleic Acid
 
 Given the rich complexity of life on Earth, it might surprise you that the
most important large molecules found in all living things from bacteria to ele-
phants can be sorted into just four main classes: carbohydrates, lipids, pro-
teins, and nucleic acids. On the molecular scale, members of three of these
classes carbohydrates, proteins, and nucleic acids are huge and are therefore
called macromolecules.
The architecture of a large biological molecule plays an essential role in
its function. Like water and simple organic molecules, large biological mole-
cules exhibit unique emergent properties arising from the orderly arrangement
of their atoms. In this chapter, we’ll first consider how macromolecules are
built. Then we’ll examine the structure and function of all four classes of large
biological molecules: carbohydrates, lipids, proteins, and nucleic acids.
This module provides variety of activities to help you understand the
basic properties and structure of cells.
BIOLOGICAL MOLECULES
The structure of carbohydrates, lipids and proteins and their roles in liv-
ing organisms
The large molecules necessary for life that are built from smaller organic mole-
cules are called biological macromolecules. There are four major classes of
biological macromolecules (carbohydrates, lipids, proteins, and nucleic acids),
and each is an important component of the cell and performs a wide array of
functions. Combined, these molecules make up the majority of a cell’s mass.
Biological macromolecules are organic, meaning that they contain carbon. In
addition, they may contain hydrogen, oxygen, nitrogen, phosphorus, sulfur,
and additional minor elements.
Molecular biology: the study of structure and functioning of biological
molecules
The Building Blocks of
Life
 Hydrogen, carbon, oxygen and nitrogen
 Monosaccharide, organic bases, amino acids, fatty acids and
glycerol
 Macromolecule: ‘giant molecule’
 Polymers (cellulose & rubber; polyester, PVC & nylon):
macromolecules made up of many repeating subunits that are
similar or identical to each other and are joined end to end
(polymerization)
 Polysaccharides
 Proteins (polypeptides)
Nucleic acids (polynucleotide
Carbon
. Carbon
 It is often said that life is “carbon-based.” This means that carbon atoms,
bonded to other carbon atoms or other elements, form the fundamental
components of many, if not most, of the molecules found uniquely in living
things.
 Other elements play important roles in biological molecules, but carbon
certainly qualifies as the “foundation” element for molecules in living
things.
 It is the bonding properties of carbon atoms that are responsible for its im-
portant role.
 
 
Carbon Bonding

Carbon contains four electrons

in its outer shell. Therefore, it
can form four covalent bonds
with other atoms or molecules.
The simplest organic carbon
molecule is methane (CH4), in Figure 2.12 Carbon can form four cova-
lent bonds to create an organic mole-
which four hydrogen atoms cule. The simplest carbon molecule is
methane (CH4), depicted here

bind to a carbon atom.

Carbohydrates
 Contains carbon, hydrogen and oxygen
 General formula: Cx(H2O)y
3 main groups:
– Monosaccharides
– Disaccharides
– Polysaccharides
Monosaccharides
 Sugars (saccharide ~ sweet or sugar)
 General formula: (CH2O)n
 Molecular and structural formula
Single sugar molecule (mono)
Types:
– Trioses (3C)
– Pentoses (5C)
– Hexoses (6C
 α -D-glucose β -D-glucose

Ring structures
• α-glucose: the form of glucose where the hydroxyl group (-OH)
on carbon atom 1 is below the ring
• β-glucose: the form of glucose where the hydroxyl group (-OH)
on carbon atom 1 is above the ring
• Isomers: 2 forms of the same chemical
Roles of Monosaccharides in Living Organisms

 First and foremost, monosaccharides are used to produce and store energy.

Most organisms create energy by breaking down the monosaccharide
glucose, and harvesting the energy released from the bonds. Other
monosaccharides are used to form long fibers, which can be used as a form
of cellular structure.
• Source of energy in respiration (glucose)
– Due to large number of carbon-hydrogen bonds which can be broken to
release energy
• Building blocks for larger molecules
– Glucose: make polysaccharides (starch, glycogen and cellulose)
– Ribose (a pentose): make RNA and ATP
– Deoxyribose (a pentose): used to make DNA
Disaccharides
and Glycosidic
Bond
• Sugars
• Condensation: how 2 monosaccharides join together to form
disaccharides
• Bridge is called glycosidic bonds
• Hydrolisis: addition of water, reverse of condensation (during
digestion of disaccharides and polysaccharides)
• Both controlled by enzymes
Polysaccharides
• Not sugars
• Polymers with monosaccharide subunits joined by condensation with glycosidic
bonds
• Several thousand monosaccharide units join to form a macromolecule
• Most important polysaccharides:
– Starch
– Glycogen Polymers of glucose
– Cellulose
• Glucose is converted to storage polysaccharides which are convenient, compact,
insoluble molecules
• In the form of starch in plants and glycogen in animals
Starch,
Glycogen and
Cellulose
 
• Starch is a mixture of amylose and amylopectin
• Amylose: many 1,4-linked α-glucose molecules form a spring
like compact structure
• Amylopectin: 1,4-linked α-glucose but shorter chains with
branching out due to 1,6 linkages
• Starch grains commonly found in chloroplast and in storage or-
gans such as the potato tuber
and the seeds of cereals and legumes
Glycogen
 
• No starch in animal cells
• Glycogen: amlyopectin-like molecules
used as the storage carbohydrates
• Glycogen molecules tend to be more
branched than amylopectin
• They clump together to form granules
– livercells and muscle cells
Cellulose
• Most abundant organic molecule (20-
40% of the average cell wall)
• Structural role (mechanically strong)
• Cellulose is a polymer of β-glucose
• Hydrogen bonds Microfibrils
Fibrils
• Very high tensile strength (almost equal to steel)
• Provide support by making tissues rigid
• Responsible for cell expansion during growth
• Freely permeable, allowing water and solutes to
reach
plasma membrane
 
Proteins
 
• >50% of the dry mass of most cells is protein
• Functions:
– Essential components of cell membranes
– The oxygen-carrying pigment haemoglobin
– Antibodies which attack and destroy invading microorganisms
– All enzymes
– Hair and the surface layers of skin contain the protein keratin
– Collagen adds strength to the many tissues, such as bone and the walls of
arteries
Amino Acids
• Basic component of protein
• Central carbon atom, amine group
(-NH2), carboxylic acid group
(-COOH)
• R group
• 20 different amino acids
 The eight amino acids in the orange area
are nonpolar and hydrophobic.
 The other amino acids are polar and
hydrophilic ("water loving").
 The two amino acids in the magenta box
are acidic ("carboxy" group in the side
chain).
• The three amino acids in the light blue box
are basic ("amine" group in the side chain).
The Peptide Bond
• 2 linked amino acids – dipeptide
• Many amino acids – polypeptide (macromolecule/polymer)
• Ribosomes – sites where amino acids are linked together to
form polypeptides
• Complete protein may contain one or more polypeptide chain
which interact with each other
Four Levels of
Protein
Structure
Primary Structure

• Linear chain of amino acids

• The types of amino acids contained in the
polypeptide chain and the sequence in
which they are joined
• Enormous number of different possible
primary structures
Secondary Structure
• Regions stabilized by hydrogen bonds
between atoms of the polypeptide backbone
• Polypeptide chain coils into an α-helix due to
attraction between the oxygen of the –CO
group of one amino acid and the hydrogen of
the -NH group of the amino acid four places
ahead of it
• This is result of the polar characteristics of
the – CO and –NH groups
• Sometimes a much looser, straighter shape
is formed, called a β-pleated sheet
Tertiary Structure
• Is the overall shape of a polypeptide resulting from
interactions between the side chains (R groups) of the
various amino acids.
• The secondary structure coils and folds to form 3
dimensional shapes
• Four types of bonds involved:
– Hydrogen bonds (between R groups)
– Disulphide bonds (between 2 cysteine molecules)
– Ionic bonds (between R groups containing amine and
carboxyl groups)
– Hydrophobic interactions (between R groups which are
non-polar or hydrophobic)
Quaternary Structure

 Is the overall protein

structure that results
from the aggregation of
these polypeptide
subunits.
 Protein consisting of
more than one amino
acid chain.
Globular and
Fibrous
Proteins
• Globular protein: protein whose molecules curl up into a ‘ball’
shape (e.g. myoglobin & haemoglobin)
• Usually curl up so that their non-polar, hydrophobic R groups
point into the centre of the molecule, away from their watery
surroundings. The polar, hydrophilic, R group remain on the
outside of the molecule
• Fibrous protein: long strands, insoluble and have structural
roles (e.g. keratin & collagen)
 Example Keratin and Colagen
 

• Molecular structure and function of haemoglobin as an

example of a globular protein
• Molecular structure and function of collagen as an example of
a fibrous protein