2.

4 PROTEINS
Essential idea
Proteins have a very wide range of functions in
living organisms
UNDERSTANDINGS
UNDERSTANDINGS
INTRODUCTION
• Proteins are an
extremely
important class of
macromolecules
in living
organisms
INTRODUCTION
•More than
50% of the
dry mass of
most cells is
protein
INTRODUCTION
• Proteins have
a wide range
of functions in
living
organisms
PROTEINS
PROTEINS
Proteins contain
•
the elements,
carbon,
hydrogen,
oxygen and
nitrogen
PROTEINS
• Proteins are
comprised of long
chains of
recurring
monomers called
amino acids
AMINO ACIDS
AMINO ACIDS
• An amino acid is made
up of a central carbon
atom bonded to:
• an amine group (NH2)
• a carboxylic acid group
(COOH)
• a hydrogen atom (H)
• a variable side chain (R)
AMINO ACIDS
• There are
20 different amino
acids found in
proteins and which
are universal to all
living organisms
AMINO ACIDS
• A further two
(selenocysteine
and pyrrolysine)
are modified
variants found only
in certain
organisms
AMINO ACIDS
• Each type of
amino acid differs
in the
composition of
the variable side
chain
AMINO ACIDS
• Two amino
acids can bind in
a condensation
reaction to form a
dipeptide
FORMATION OF A
PEPTIDE BOND
Skill
Drawing molecular diagrams to show the
formation of a peptide bond
FORMATION OF A PEPTIDE BOND
• Amino acids can be
covalently joined
together in a
condensation
reaction to form a
dipeptide and
water
FORMATION OF A PEPTIDE BOND
• A dipeptide is a
molecule
consisting of two
amino acids
linked by a
peptide bond
FORMATION OF A PEPTIDE BOND
• In the formation of a
dipeptide, one amino
acid loses a hydroxyl
(–OH) group from its
carboxylic acid group,
while the other loses a
hydrogen atom from its
amine group
FORMATION OF A PEPTIDE BOND
• The link formed
between the
two amino acids
is called a
peptide bond
DRAWING PEPTIDE
BONDS
Skill
Drawing molecular diagrams to show the
formation of a peptide bond
DIVERSITY OF AMINO
ACIDS
Understanding
• There are 20 different amino acids in polypeptides
synthesized on ribosomes
• Amino acids can be linked together in any sequence
giving a huge range of possible polypeptides
DIVERSITY OF AMINO ACIDS
• There are
20 different
amino acids
found in
proteins
DIVERSITY OF AMINO ACIDS
• The 20 amino
acids can be
linked together in
any sequence to
form polypeptides
DIVERSITY OF AMINO ACIDS
• Theoretically, 20n
different types of
polypeptides can be
formed, where n is
the number of
amino acids per
polypeptide
DIVERSITY OF AMINO ACIDS
• Synthesis of
polypeptides
takes place on
ribosomes, in a
process called
translation
FORMATION OF
POLYPEPTIDES
Understanding
Amino acids are linked together by condensation to form
polypeptides
Amino acids can be linked together in any sequence
giving a huge range of
possible polypeptides
FORMATION OF POLYPEPTIDES
• Any number of extra
amino acids could be
added to the dipeptide
chain in a series of
condensation
reactions to form a
molecule called a
polypeptide
FORMATION OF POLYPEPTIDES
• Polypeptides are
chains of amino acids
that are made by
linking together amino
acids by peptide
bonds via
condensation
reactions
FORMATION OF POLYPEPTIDES
• The sequence of
amino acids linked
together in a
polypeptide chain
determines the type
of polypeptide
formed
GENES AND
POLYPEPTIDES
Understanding
The amino acid sequence of polypeptides is
coded for by genes
GENES AND POLYPEPTIDES
• A gene is a
short length of
DNA that
provides the
code for making
one polypeptide
GENES AND POLYPEPTIDES
• The order of the
amino acids in a
polypeptide is
controlled by
the gene
GENES AND POLYPEPTIDES
• The instruction for
making a particular
kind of polypeptide
is carried to the
ribosome where the
polypeptide is made
POLYPEPTIDES AND
PROTEINS
Understanding
A protein may consist of a single polypeptide
or more than one polypeptide linked together
POLYPEPTIDES AND PROTEINS
• A complete protein
molecule may
contain just one
polypeptide chain, or
it may have two or
more chains which
interact with each
other
SOME PROTEINS AND THE NUMBER OF
POLYPEPTIDE CHAINS THEY ARE MADE
OF
Understanding
A protein may consist of a single polypeptide or
more than one polypeptide linked together
CONFORMATION OF
POLYPEPTIDES
Understanding
The amino acid sequence determines the
three-dimensional conformation of a protein
CONFORMATION OF POLYPEPTIDES
• The order of the
amino acids in a
polypeptide
determines the
shape and function
of the protein
CONFORMATION OF POLYPEPTIDES
• The R groups of the
amino acids
determine the types
of bonds and
interactions with
other molecules
CONFORMATION OF POLYPEPTIDES
• The R groups
interactions defines how
the polypeptide chain or
chains fold up in the
protein and so directly
affect its three-
dimensional structure,
known as its
conformation
CONFORMATION OF POLYPEPTIDES
• The sequence or
order of amino
acids in a
polypeptide forms
the primary
structure
CONFORMATION OF POLYPEPTIDES
• The folding of
polypeptide chains
into β-pleated
sheets or α-helices
forms its
secondary
structure
CONFORMATION OF POLYPEPTIDES
• The folding and
coiling of
polypeptide chains
into a complex
three-dimensional
shape forms its
tertiary structure
CONFORMATION OF POLYPEPTIDES
• More than one
polypeptide chain can
be linked together with
the multiple subunits
being held together in
a multi-subunit
complex to form the
quaternary structure
CONFORMATION OF POLYPEPTIDES
• A single change in the
order of amino acids
can cause changes in
a protein's
conformation, resulting
in a change of
shape or loss of
function
DENATURATION OF
PROTEINS
Application
Denaturation of proteins by heat or by deviation of
pH from the optimum
DENATURATION OF PROTEINS
• It is the change in
the conformation
(three-dimensional
structure) of a
protein or
polypeptide
DENATURATION OF PROTEINS
• It results from the
disruption of the
bonds or interactions
between the R
groups within the
molecule that
stabilize the protein
DENATURATION OF PROTEINS
• The disruption of the
interaction between the
R groups irreversibly
changes the quaternary
and tertiary structures
(and in some extreme
conditions the
secondary structures)
DENATURATION OF PROTEINS
• Denaturation of
proteins can usually
be caused by two
key conditions or
factors
• temperature and
• pH
HOW TEMPERATURE CAUSES
DENATURATION OF PROTEINS
Application
Denaturation of proteins by heat or by deviation of
pH from the optimum
HOW TEMPERATURE CAUSES DENATURATION
OF PROTEINS
• Extreme heat can
cause vibrations
within the molecule
that breaks
intermolecular
bonds or
interactions
HOW TEMPERATURE CAUSES DENATURATION
OF PROTEINS
• As these bonds
are broken, the
protein will begin
to unfold and lose
its capacity to
function as
intended
HOW TEMPERATURE CAUSES DENATURATION
OF PROTEINS
• Temperatures
at which
proteins
denature may
vary
HOW pH CAUSES
DENATURATION OF PROTEINS
Application
Denaturation of proteins by heat or by deviation of
pH from the optimum
HOW pH CAUSES DENATURATION OF
PROTEINS
• Extremes of pH (strong
acids or alkali) may
cause denaturation by
breaking or forming
ionic bonds within the
molecule, changing the
three-dimensional
structure of the protein
PROTEOME
Understanding
Every individual has a unique proteome
PROTEOME
• The proteome is
the totality of
proteins within a
cell, tissue or
organism at a
certain time
PROTEOME
It is all the
•
proteins
produced by a
cell, tissue or
organisms
PROTEOME
• Within a species,
there are strong
similarities in the
proteome of all
individuals, but
also differences
PROTEOME
• The proteome of each
individual is unique
because of:
• differences of activity
• small differences in
the amino acids
sequences of
proteins
PROTEOME
Thus every
•
individual has a
unique
proteome which
is different from
all others
IMPORTANCE OF
PROTEOME
Understanding
Every individual has a unique proteome
IMPORTANCE OF PROTEOME
• Proteome
analysis has
become a new
tool in medical
research and
cancer treatment
IMPORTANCE OF PROTEOME
• To treat certain cancers,
the proteome of a
patient's cancer cells is
analysed to determine if
a particular
chemotherapy will be
successful
PROTEINS FUNCTIONS IN
LIVING ORGANISMS
Essential idea
Proteins have a very wide range of functions in
living organisms
CATALYSIS OF METABOLISM
• All enzymes are
proteins and
catalyse specific
reactions inside
or outside the
cell
MUSCLE CONTRACTION
• Actin and myosin
are proteins that
cause contraction of
muscles used in
locomotion and
transport around the
body
FORMATION OF CYTOSKELETON
• Tubulin is a protein
that forms the subunits
of microtubules that
give animal cells their
shape and pull on
chromosomes during
mitosis
PROVISION OF TENSILE STRENGTH
• Fibrous proteins
give tensile strength
needed in the skin,
tendons, ligaments,
and blood vessel
walls
BLOOD CLOTTING
• Blood proteins act
as clotting factors
that cause blood
to turn from liquid
to a gel in
wounds
TRANSPORT OF NUTRIENTS AND GASES
• Proteins in blood
(e.g. haemoglobin)
helps to transport
oxygen, carbon
dioxide, iron and
lipids
ADHESION OF CELLS
• Membrane
proteins cause
adjacent animal
cells to stick to
each other within
tissues
MEMBRANE TRANSPORT
• Membrane proteins
are used for facilitated
diffusion, active
transport and also for
electron transport
during respiration and
photosynthesis
MAKING OF HORMONES
• Some
hormones such
as insulin, FSH
and LH are
proteins
RECEPTORS
• Glycoproteins serve as
binding sites in
membranes and
cytoplasm for
neurotransmitters,
hormones, tastes and
smells and also
receptors for light in the
eye and in plants
PACKING OF DNA
• Histones are proteins
associated with the
DNA in eukaryotes
and helps the DNA to
supercoil into
chromosomes during
mitosis
IMMUNITY
• Antibodies are
proteins produced
by lymphocytes to
destroy
pathogens and
their antigens
SOME PROTEINS AND
THEIR FUNCTIONS
Essential idea
Proteins have a very wide range of functions in
living organisms
BIBLIOGRAPHY / ACKNOWLEDGMENTS
END OF UNIT