The Structure and Function of Macromolecules:

Carbohydrates, Lipids, Phospholipids & Nucleic

Acids
 The FOUR Classes of Large Biomolecules

• All living things are made up of four classes of

large biological molecules:
• Carbohydrates
• Lipids
• Protein
• Nucleic Acids

• Macromolecules are large molecules composed

of thousands of covalently bonded atoms

• Molecular structure and function are inseparable

 The FOUR Classes of Large Biomolecules

• Macromolecules are polymers, built

from monomers
• A polymer is a long molecule consisting of many
similar building blocks
• These small building-block molecules are called
monomers
The synthesis and breakdown of polymers

• A dehydration reaction occurs when two

monomers bond together through the loss
of a water molecule. “To put together while
losing water.”
• Polymers are disassembled to monomers
by hydrolysis, a reaction that is essentially
the reverse of the dehydration reaction
Means splitting of chemical bonds by
addition of water.
Dehydration Synthesis
Hydrolysis
Dehydration and hydrolysis reactions are
catalyst, or “sped up”, by specific
[Link] reactions involved the
formation of new bonds requiring energy, while
hydrolysis reactions break bonds and release
energy.
 The Diversity of Polymers

• Each cell has thousands of different

macromolecules

• Macromolecules vary among cells of an

organism, vary more within a species, and vary
even more between species

• An immense variety of polymers can be built

from a small set of monomers
 Carbohydrates Serve as Fuel
& Building Material

• Carbohydrates include sugars and the polymers

of sugars

• The simplest carbohydrates are

monosaccharides, or single sugars

• Carbohydrate macromolecules are

polysaccharides, polymers composed of many
sugar building blocks
• Carbohydrates can be represented by a
stoichiometric formula (CH2O)n, where n is the
number of carbons in the molecule.
• Ratio [Link]
• Carbon (“carbo”) and the components of
water.
 Sugars: Monosaccharides
• Monosaccharides have molecular
formulas that are usually multiples of
CH2O

• Glucose (C6H12O6) is the most

common monosaccharide

• Monosaccharides are classified by

– The location of the carbonyl group
– The number of carbons in the
carbon skeleton
• In monosaccharides, the number of carbons
usually ranges from three to [Link]
names end with suffix –ose.
• If the sugar has an aldehyde group (R-CHO),it
is know as an aldose.
• If ketone group (RC(=O)R’), it is known as
ketose.
• Depending on the number of carbons in the
sugar, they also may be known as trioses,
pentoses and or hexoses.
• When alpha-glucose molecules are joined
chemically to form a polymer starch is formed.
When beta-glucose molecules are joined to
form a polymer cellulose is formed.
 Examples of Monosaccharides
a. Glucose –also known as dextrose or grape
sugar is the only form of sugar used by the body
that provides energy to fuel all cellular
processes. It is the most abundant carbohydrate
in the blood that is why it is also called blood
sugar. It requires no digestion and may be given
intravenously to patients who cannot take food
by mouth. Glycosuria is the term for glucose
present in urine.
b. Fructose or levulose – is considered the
sweetest among the sugar being twice as sweet
as glucose. It is found in fruits, honey and corn
syrups. It is metabolized directly, but is also
readily converted to glucose in the liver.
c. Galactose or aldohexose – is obtained from
milk and an important component that serves as
a marker that can help identify blood types. It is
less than half as sweet as glucose. A genetic
metabolic disorder(usually for infants) that
affects how the body processes galactose is
known as galactosemia.
GALT
 Sugars: Disaccharides
• A disaccharide is formed when a dehydration
reaction joins two monosaccharides

• This covalent bond is called a glycosidic linkage

 Examples of Dissacharides
a. Sucrose – commonly known as table sugar is
a combination of glucose and fructose and is
considered an excellent natural preservative.
b. Lactose – found in milk and milk products is
formed by combining glucose and galactose.
An enzyme called lactase is needed to digest
this. Lactose intolerance is common digestive
disorder where the body cannot fully digest
lactose.
c. Maltose- found in beer is composed of two
glucose. It also provides energy germinating
seeds.
Synthesizing Maltose ,Galactose
and Sucrose
 Polysaccharides
• Polysaccharides, the polymers of sugars,
have storage and structural roles

• The structure and function of a polysaccharide

are determined by its sugar monomers and
the positions of glycosidic linkages
 Types of Polysaccharides: Storage

• Starch, a storage
polysaccharide of
plants, consists
entirely of glucose
monomers
• Plants store surplus
starch as granules
within chloroplasts
and other plastids
• The simplest form of
starch is amylose
• Made up of a mixture of amylose and
amylopectin (polymers of glucose).
• Hydrolysis is the major chemical reaction in
the digestion of starchy food. Ptyalin or
salivary amylase is the enzyme that changes
starch into sugar.
Starch made up of glucose monomers that are joined by
alpha 1-4 or 1-6 glycosidic bond.
 Types of Polysaccharides: Storage
• Glycogen is a storage
polysaccharide in
animals
• Humans and other
vertebrates store
glycogen mainly in liver
and muscle cells
• Whenever blood
glucose level decrease,
glycogen is broken
down to release
glucose in a process
known as
glycogenolysis.
 Types of Polysaccharides: Structural

• The polysaccharide cellulose is a major

component of the tough wall of plant [Link]
abundant biopolymer.

• Like starch, cellulose is a polymer of glucose,

but the glycosidic linkages differ

• The difference is based on two ring forms for

glucose: alpha () and beta ()
• Beta 1,4 linkage in cellulose cannot be broken
by human digestive enzymes, herbivores such
as cows, koalas, buffalos, and horses able to
digest in their stomach.
• Cellulases can break down cellulose into
glucose monomers.
Cellulose: A termite’s best friend!

Note the
H-bonds
Such Elegance!
 Types of Polysaccharides: Structural

• Chitin, another structural polysaccharide, is found

in the exoskeleton of arthropods (insects,
crustaceans,and others) .

• Chitin also provides structural support for the cell

walls of many fungi.

• Polysaccharide-containing [Link] is made up of

repeating units of N-acetyl-β-D-glucosamine, a modified
sugar.
Who knew?
LIPIDS
 Lipids Are Hydrophobic
Lipids are a diverse group of hydrophobic
molecules
• Lipids are the one class of large biological
molecules that do not form polymers
• The unifying feature of lipids is having little or no
affinity for water (water fearing)
• Lipids are hydrophobic because they consist
mostly of hydrocarbons, which form nonpolar
covalent bonds
• The most biologically important lipids are fats,
phospholipids, and steroids
 Fats and Oils
• Fat molecule consists mainly of two
components- glycerol and fatty acids.
• Glycerol is an organic compound (alcohol)
with three carbons, five hydrogens, and three
hydroxyl (OH) groups.
• Fatty acids – have a long chain of
hydrocarbons to which carboxyl group is
attached, hence the name fatty acid.
 Fats: Start with a Simple Little
Glycerol Molecule

• Fats are constructed from two

types of smaller molecules:
glycerol and fatty acids
• Glycerol is a three-carbon alcohol
with a hydroxyl group attached to
each carbon
• A fatty acid consists of a carboxyl
group attached to a long carbon
skeleton
• The number of carbons in fatty acid may range
from 4 to 36; most common are those
containing 12-18 carbons.
• Fatty acids are attached to each three carbons
of the glycerol molecule with an ester bond
through an oxygen atom.
 Dehydration Rxn 1: Add a Fatty Acid

• Next, add a “fatty acid” through a dehydration

synthesis reaction
• What makes it an acid? The C double bond O,
single bond OH!
 Dehydration Rxn 2!!

• Next, add a SECOND “fatty acid” through a

dehydration synthesis reaction
 Dehydration Reaction THREE!!!

• The joining
of the C of
the fatty acid
to the O of
the hydroxyl
group of the
glycerol is
called an
ester
linkage.
• Fats are also called triacylglycerols or
triglycerides because of their chemical
structure.
• Ex. Palmitic acid, a saturated fatty acid derived
from the palm tree and arachidic acid is
derived from Arachis hypogea, the scientific
name of groundpeanuts of peanuts.
Saturated /Unsaturated Fatty Acids
• Saturated - If there are only single bonds
between neighboring carbons in the hydrogen
carbon chain. Saturated by hydrogen;the
number of hydrogen atoms attached to the
carbon skeleton is maximized.
• Long straight fatty acids with single bonds
tend to get packed tightly and are solid at
room temperature.
• Ex. Stearic acid, palmitic acid and the fat with
butyric acid (common in butter)
• Stearic acid
• Mammals store fats in specialized cells called
adipocytes, where globules of fat occupy most
of the cells volume. In plants, fat or oil is
stored in many seeds and is used as a source
of energy during seedling development.
• Unsaturated- When the
hydrocarbon chain contains a
double bond, the fatty acid is said
to be unsaturated.
• Oleic acid
• Most unsaturated are liquid in room
temperature and are called oils.
• If there is one double bond in the molecule, it
is known as monounsaturated fat (ex. Olive
oil).
• If there is more than one double bond ,it is
known as a polyunsaturated fat (ex. Canola oil)
• Usually of plant origin and contain cis
unsaturated fatty acids.
• Cis and trans indicate the configuration of the
molecule around the double bond.
• If the hydrogens are present in the same
plane, it is referred to as cis fat; if the
hydrogen atoms are on two different planes, it
is called trans fat.
• The cis double bond causes a bend of a ‘kink’
that prevents the fatty acids from packing
tightly, keeping them liquid in temperature.
• Olive oil , corn oil, canola oil, and cod liver oil
contain unsaturated fats.
• Unsaturated fats help to lower blood
cholesterol levels; whereas, saturated fats
contribute to plaque formation in the arteries.
 Trans Fat
• In food industry, oils are artificially
hydrogenated to make them semi-solid and of
a consistency desirable for many processed
food products.
• Hydrogen gas is bubbled through oils to
solidify them.
• During hydrogenation process, double bonds
of the cis- conformation in the hydrocarbon
chain may be converted to double bonds in
trans-conformation.
• Margarines, some types of peanut butter, and
shortening contain artificially hydrogenated
trans fats.
• Increase in trans fats in the human diet may
lead to an increase in levels of low-density
lipoproteins (LDL), or bad cholesterol.
 Omega Fatty Acids
• Essential fatty acids- are fatty acids required
but not synthesized by the human [Link]
to be supplemented through ingestion.
• Omega-3 fatty acids - one of only two known
essential fatty acids for humans (the other
being omega 6- fatty acid).Called as
polyunsaturated fatty acid because the third
carbon from the end of the hydrocarbon chain
is connected to its neighbouring carbon by
double bond.
• Alpha-linolenic acid
• The farthest carbon away from the carboxyl
group is numbered as the omega (ω) carbon.
• If the double bond is between the third and
fourth carbon from that end, it is known as an
omega-3 fatty acid.
• Omega-3 fatty acids include alpha linoleic acid
(ALA), eicosapentaenoic aicd (EPA), and
decosahaxaenoic acid (DHA), all of which are
polyunsaturated.
• Salmon, trout, and tuna are good sources.
• Reduce the risk of sudden death from heart
attacks, reduce triglycerides in the blood,
lower blood pressure, and prevent thrombosis
by inhibiting blood [Link] reduce
inflammation, and may help reduce the risk of
some cancers in animals.
 WAXES
• Was covers the feathers of some aquatic birds
and the leaf surfaces of some plants.
• Because of the hydrophobic nature of waxes,
they prevent water from sticking on the
surface.
• Waxes are made up of long fatty acid chains
esterified to long-chain alcohol.
 Phospholipids
• Major constituents of plasma membrane.
• Composed of fatty acid chains attached to a
glycerol or sphingosine backbone.
• Two fatty acids connected to the chains form
the diacyglycerol.
• The third carbon of the glycerol backbone is
modified by a phosphate group
• A phosphate group alone attached to a
diacylglycerol does not qualify as a
phospholipid; it is a phosphatidate
(diacylgycerol 3-phosphate) , the precursor of
phospholipids.
• Amphiphathic molecule.
• If a drop of phospholipids is placed in water, it
spontaneously forms a structure known as
micelle.
• Phosphotadylcholine (PC) and
phosphotadylserinec (PS) are two important
phospholipids that are found in plasma
membrane.
• Phosphotadylcholine – eggs,
soybeans ,mustard, sunflower and other
foods.
• Phosphotadylserine- meat and fish
 Steroids
• Have fused ring structure.
• All steroids have four linked carbon rings and
several of them , like cholesterol have short
tail.
• -OH functional group which put them in the
alcohol classification (sterols).
• Cholesterol is the most common steroid. It is
mainly synthesized in the liver and is precursor
to many steroid hormones such as
testosterone and estradiol, which are secreted
by gonads and endocrine glands.
• Pecursor to vitamin D and bile salts
PROTEINS
 Proteins
• One of the most abundant organic molecules
in living systems and have the most diverse
range of functions of all macromolecules.
• Functions ; structural, regulatory, contractile,
or protective, or they may be toxins or
enzymes.
• Polymers of amino acids, arranged in a linear
sequence.
 Enzyme
ENZYMES
• Important proteins in a biological
[Link] by living cells, are catalysts
in biochemical reactions (like digestion) and
are usually complex or conjugated proteins.
• May help in breakdown ,rearrangement, or
synthesis reactions.
• Enzymes that break down their substrates are
called catabolic enzymes.
• Enzymes that build more complex molecules
from their substrates are called anabolic
enzymes.
• Enzymes that affect the rate of reaction are
called catalytic enzymes.
• An enzyme will bind with the substrate in an
area on the enzymes surface called the active
site, forming substrate-enzyme complex.
• All enzymes increase the rate of reaction and,
therefore, are considered to be organic
catalysts.
• An example of an enzyme is salivary amylase,
which hydrolyzes its substrate amylose, a
component of starch.
• Enzyme is specific for the substrate it acts on,
such that their active sites have very precise
shapes, that only one substrate can fit in each
site and is chemically attracted to it(enzyme-
substrate specificity).
• Rates of enzyme reactions are also affected by
different factors such as : temperature, pH and
amount of substrate.
 Temperature
• Chemical reactions increase as temperature
also increases because the reacting molecules
move faster and collide more often.
• However, as the temperature continues to
increase beyond the optimum temperature,
enzyme denaturation occurs.
• Optimum temperature : human- 37 , bacteria-
65.
 pH
• Indicates acidity/ basicity of a solution,
actually measures the H ions (H+).
• The lower the pH, the higher the
concentration of H+ ions there is.
• These ions affect the existing chemical bonds
in an enzyme and therefore affects its shape,
including that of the active site.
• Human pH between 6-8, pepsin(in acidic
stomach) pH 1-4 , and trypsin (alkali small
intestine) pH 8.
 Substrate Concentration
• Enzyme activity increases as substrate concentration
increases, but as long as there are 3 active sites
available.
• Increase in substrate concentration increases
collision between the substrate and enzyme
molecules.
• Once all the enzyme active sites are engaged with
the substrate molecules, the reaction rate levels off,
despite continued increase in substrate
concentration.
• The active site is said to be saturated with substrate,
and thus called the saturation point.
 Amino Acids
• Monomers that make up proteins.
• Each amino acid has the same fundamental
structure, which consists of a central carbon
atom, also known as alpha(α)carbon, bonded
to an amino group (NH2), a carboxyl group
(COOH), and to hydrogen atom.
• Every amino acid also has another atom or
group of atoms known as R group bonded to
the central carbon atom.
• The name amino acid is derived from the
amino group and the carboxyl group that
make up amino acid.
• There are 20 amino acids present in proteins.
(Ten of these are considered essential amino
acids in humans because the human body
cannot produce them, and they are obtained
from diet.).
• For each amino acid, the R group(or side
chain) is different.
• The chemical nature of the side chain
determines the nature of the amino acid.
• Ex. Valine, methionine, and alanine are
nonpolar of hydrophobic in nature., while
serine, threonine, and cysteine are polar and
have hydrophilic side chains. The side chains
of lysine and arginine are positively charged,
therefore , these amino acids are also known
as basic amino acids.
• Proline has an R group linked to the amino
group, froming a ring-like [Link] is
an exception to the standard structure of an
amino acid, since its amino group is not
separate from the side chain.
• Amino acid and sequence and the number of
amino acids in the polypeptide chain
ultimately determine the protein’s shape, size,
and function.
• Each amino acid is attached to another amino
acid by a covalent bond, known as peptide
bond, which is formed by dehydration
reaction.
• The carboxyl group of one amino acid and the
amino group of the incoming amino acid
combine, releasing a molecule of water.
• Products formed by such linkages are called
peptides.
• As more amino acids join to this growing
chain, the resulting chain is known
polypeptide.
• Each polypeptide has a free amino group at
one end. This end is called N-terminus ,or the
amino terminus.
• The other end has a free carboxyl group, also
known as the C or carboxyl terminus.
• Polypeptide- a polymer of amino acids.
• Protein- used for a polypeptide or
polypeptides that have combined together;
often have bound non peptide prosthetic
groups, distinct shape, and a unique function.
• After protein synthesis(translation) , most
proteins are modified. These are known post –
translational modifications. They may undergo
cleavage, phosphorylation, or may require the
addition of other chemical groups. Only after
these modifications is the protein completely
functional.
 Primary Structure
• The unique sequence of amino acids in a
polypeptide chain.
• Ex. Pancreatic hormone of insulin has two
polypeptide chain, A and B, and they are
linked together by disulfide bonds. The N
terminal amino acid of the A chain is glycine,
whereas the C terminal acid is asparagine.
• A change in nucleotide sequence of the gene’s
coding region may lead to a different amino
acid being added to growing polypeptide
chain , causing a change in protein structure
and function.
• Ex. Sickle cell anemia, the hemoglobin β chain
has a single amino acid substitution , causing a
change in protein structure and function.
• Glutamic acid is substituted by valine.
 Secondary Structure
• The local folding of the polypeptide in some
regions.
• The most common are the α-helix and β-
pleated sheet structures.
• In the α-helix structure, the helix is held in
shape by hydrogen bonds. Hydrogen bonds
form between the oxygen atom in the
carbonyl group in one amino acid and
another amino acid that is four amino acids
farther along the chain.
• Β-pleated sheet, the pleat are formed by
hydrogen bonding between atoms on the
backbone of the polypeptide chain. The R
groups are attached to the carbons and
extend above and below the folds of the pleat.
 Tertiary Structure
• The unique three dimensional structure of a
polypeptide .This structure is in part due to
chemical interactions at work on the
polypeptide chain.
 Quarternary Structure
• In nature, some proteins are formed from
several polypeptides and the interaction of
these subunits forms the quarternary
structure.
NUCLEIC ACIDS
 Nucleic Acids
• The most important macromolecules for the
continuity of life.
• They carry the genetic blueprint of a cell and
carry instructions for the functioning of the
cell.
• Two main types of nucleic acids are DNA and
RNA.
 DNA
• The genetic material found in all organisms,
ranging from single-celled bacteria to
multicellular mammals.
• It is found in the nucleus of eukaryotes and in
the chloroplasts and mitochondria.
• In prokaryotes, the DNA is not enclosed in a
membranes envelop.
• Controls all of the cellular activities by turning
the genes “on” or “off” .
 RNA
• Another type of nucleic acid and is mostly
involved in protein synthesis.
• Other types of RNA- like mRNA, tRNA, and
microRNA – are involved in protein synthesis
and its regulation.
• DNA and RNA are made up of monomers
known as nucleotides.
• The nucleotides combine with each other to
form a polynucleotide, DNA or RNA.
• Each nucleotide is made up of three
components : a nitrogenous base, a pentose
(five-carbon) sugar, and a phosphate group.
• Each nitrogenous base is attached to one or
more phosphate groups.
 Nitrogenous bases
• Important components of nucleotides,are
organic molecules, and named because they
contain carbon and nitrogen.
• They are bases because they contain an amino
group that has the potential of binding an
extra hydrogen.
• Adenine, Guanine , Cytosine, and Thymine.
• Adenine and Guanine are considered as
purines.
• The primary structure of a purine is two
carbon-nitrogen ring represented by adenine
and guanine.
• Cytosine, thymine, and uracil on the other
hand are classified as pyrimidines which have
a single carbon ring as their primary structure.
• In DNA is deoxyribose, and in RNA, the sugar is
ribose.
• The difference between the sugars is the
presence of the hydroxyl group on the second
carbon of the deoxyribose.
• The phosphate residue is attached to the
hydroxyl group of the 5’ carbon of one sugar
and the hydroxyl group of the 3’ carbon of the
sugar of the next nucleotide, which forms a 5’-
3’.
• The phosphodiester linkage is not formed by
simple dehydration [Link]’s formation
involves the removal of two phosphate
groups.
• A polynucleotide may have a thousands of
phosphodiester linkages.
 DNA DOUBLE-HELIX STRUCTURE
• DNA has a double helix structure.
• The phosphate lie on the outside of the helix,
forming backbone of the DNA.
• The nitrogenous bases are stacked in the
interior, like the steps of the staircase, in pairs;
the pairs are bound to each other by hydrogen
bonds.
• The two strands of the helix run in opposite
directions, meaning that the 5’ carbon end of
one strand will face 3’ carbon end of its
matching strand. (antiparallel orientation)
• Certain purine can only pair with a certain
[Link] as the base complementary
rule or Chargaff’s Rule.
• Ex. 5’ AATTGGCC 3’
3’ TTAACCGG 5’ complimentary strand
 RNA
• Protein synthesis under the direction of DNA.
• Single stranded and is made of
ribonucleotides that are linked by
phosphodiester bonds.
• A,U,G,C nitrogenous base, ribose, and
phosphate group
 4 types of RNA
• Messenger RNA (mRNA)- carries message
from DNA which controls all of the cellular
activities in the cell.
• The mRNA is read in sets of three bases
known as codons.
• Ribosomal RNA (rRNA)- is a major constituent
of the ribosomes on which the mRNA [Link]
ensures the proper alignment of the mRNA
and the [Link] has also a an enzymatic
activity ( peptidyl tranferase) and catalyzes the
formation of the peptide bonds between two
aligned amino acids.
• Transfer RNA (tRNA)- It carries the correct
amino acid to the site of protein synthesis.
• MicroRNAs (miRNA)- Involves the regulation
of gene expression by interfering with the
expression of certain mRNA messages.