UNIT-I

MACROMOLECULES
IN CELL
 MOLECULAR COMPOSITION OF CELLS
⦿ Cells are composed of water, inorganic ions, and carbon-containing
(organic) molecules.
⦿ Water is the most abundant molecule in cells, accounting for 70% or
more of total cell mass.
⦿ The inorganic ions of the cell, including sodium (Na+), potassium (K+),
magnesium (Mg2+), calcium (Ca2+), phosphate (HPO42-), chloride (Cl-),
and bicarbonate (HCO3-), constitute 1% or less of the cell mass. 
⦿ However, organic molecules are the unique constituents of cells. Most of
these organic compounds belong to one of four classes of molecules:
carbohydrates, lipids, proteins, and nucleic acids.
⦿ Proteins, nucleic acids, and most carbohydrates (the polysaccharides)
are macromolecules formed by the joining (polymerization) of hundreds
or thousands of low-molecular-weight precursors: amino acids,
nucleotides, and simple sugars, respectively. Such macromolecules
constitute 80 to 90% of the dry weight of most cells. Lipids are the other
major constituent of cells. 
STRUCTURE OF SIMPLE SUGARS

Representative sugars containing three, five, and six

carbons (triose, pentose, and hexose sugars,
respectively) are illustrated. Sugars with five or
more carbons can cyclize to form rings, which exist
in two alternative forms (α and β) depending on the
configuration of carbon 1.
CARBOHYDRATES
 CARBOHYDRATES
⦿ The carbohydrates include simple sugars as well as polysaccharides.
⦿ These simple sugars, such as glucose, are the major nutrients of cells. Their breakdown
provides both a source of cellular energy and the starting material for the synthesis of other
cell constituents.
⦿ Polysaccharides are storage forms of sugars and form structural components of the cell
⦿ Polysaccharides and shorter polymers of sugars act as markers for a variety of cell
recognition processes, including the adhesion of cells to their neighbors and the transport of
proteins to appropriate intracellular destinations.
⦿ The basic formula for these molecules is (CH2O)n, from which the name carbohydrate is
derived (C= “carbo” and H2O= “hydrate”).
⦿ The six-carbon (n= 6) sugar glucose (C6H12O6) is especially important in cells, since it
provides the principal source of cellular energy.
⦿ Other simple sugars have between three and seven carbons, with three- and five-carbon
sugars being the most common.
⦿ Sugars containing five or more carbons can cyclize to form ring structures, which are the
predominant forms of these molecules within cells. Cyclized sugars exist in two alternative
forms (called α or β), depending on the configuration of carbon 1.
CARBOHYDRATES
⦿ Monosaccharides can be joined together by
dehydration reactions, in which H2O is removed
and the sugars are linked by a glycosidic
bond between two of their carbons
⦿ If only a few sugars are joined together, the
resulting polymer is called an oligosaccharide.
⦿ If a large number (hundreds or thousands) of
sugars are involved, the resulting polymers are
macromolecules called polysaccharides.
FORMATION OF A GLYCOSIDIC BOND
Two simple sugars are
joined by a dehydration
reaction (a reaction in
which water is
removed). In the
example shown, two
glucose molecules in the
α configuration are
joined by a bond
between carbons 1 and
4, which is therefore
called an α (1→4)
glycosidic bond.
 CARBOHYDRATES
⦿ Two common polysaccharides—glycogen and starch—are the
storage forms of carbohydrates in animal and plant cells,
respectively.
⦿ Both glycogen and starch are composed entirely of glucose
molecules in the α configuration
⦿ The principal linkage is between carbon 1 of one glucose and
carbon 4 of a second.
⦿ In addition, both glycogen and one form of starch
(amylopectin) contain occasional α (1→6) linkages, in which
carbon 1 of one glucose is joined to carbon 6 of a second.
⦿ These linkages lead to the formation of branches resulting
from the joining of two separate α (1→4) linked chains.
⦿ Such branches are present in glycogen and amylopectin,
although another form of starch (amylose) is an unbranched
molecule.
 STRUCTURE OF POLYSACCHARIDES

Polysaccharides are macromolecules consisting of hundreds or thousands of simple sugars.

Glycogen, starch, and cellulose are all composed entirely of glucose residues, which are joined by
α (1→4) glycosidic bonds in glycogen and starch but by β (1→4) bonds in cellulose. Glycogen and
one form of starch (amylopectin) also contain occasional α (1→6) bonds, which serve as branch
points by joining two separate α (1→4) chains.
CARBOHYDRATES
⦿ Structures of glycogen and starch are thus basically similar, as is their
function: to store glucose. 
⦿ Cellulose, in contrast, has a quite distinct function as the principal
structural component of the plant cell wall.
⦿ Cellulose is also composed entirely of glucose molecules. The glucose
residues in cellulose, however, are in the β rather than the α
configuration, and cellulose is an unbranched polysaccharide 
⦿ The linkage of glucose residues by β (1→4) rather than α (1→4) bonds
causes cellulose to form long extended chains that pack side by side to
form fibers of great mechanical strength.
⦿ In addition to their roles in energy storage and cell structure,
oligosaccharides and polysaccharides are important in a variety of cell
signaling processes. For example, oligosaccharides are frequently linked
to proteins, where they serve as markers to target proteins for transport
to the cell surface or incorporation into different subcellular organelles.
⦿ Oligosaccharides and polysaccharides also serve as markers on the
surface of cells, playing important roles in cell recognition and the
interactions between cells in tissues of multicellular organisms.
LIPIDS

 LIPIDS
⦿ Lipids have three major roles in cells.
⦿ First, they provide an important form of energy storage.
⦿ Second, and of great importance in cell biology, lipids are the major components
of cell membranes.
⦿ Third, lipids play important roles in cell signaling, both as steroid
hormones (e.g., estrogen and testosterone) and as messenger molecules that
convey signals from cell surface receptors to targets within the cell.
⦿ The simplest lipids are fatty acids, which consist of long hydrocarbon chains,
most frequently containing 16 or 18 carbon atoms, with a carboxyl group (COO-)
at one end
⦿ Unsaturated fatty acids contain one or more double bonds between carbon
atoms; in saturated fatty acids all of the carbon atoms are bonded to the
maximum number of hydrogen atoms.
⦿ The long hydrocarbon chains of fatty acids contain only nonpolar C—H bonds,
which are unable to interact with water.
⦿ The hydrophobic nature of these fatty acid chains is responsible for much of the
behavior of complex lipids, particularly in the formation of biological
membranes.
STRUCTURE OF FATTY ACIDS
⦿ Fatty acids consist of
long hydrocarbon chains
terminating in a
carboxyl group (COO-).
⦿ Palmitate and stearate
are saturated fatty
acids consisting of 16
and 18 carbons,
respectively.
⦿ Oleate is an unsaturated
18-carbon fatty acid
containing a double
bond between carbons 9
and 10. Note that the
double bond introduces
a kink in the
hydrocarbon chain.
 LIPIDS
⦿ Fatty acids are stored in the form of triacylglycerols,
or fats, which consist of three fatty acids linked to a
glycerol molecule
⦿ Triacylglycerols are insoluble in water and therefore
accumulate as fat droplets in the cytoplasm. When
required, they can be broken down for use in energy-
yielding reactions.
⦿ It is noteworthy that fats are a more efficient form of
energy storage than carbohydrates, yielding more
than twice as much energy per weight of material
broken down.
⦿ Fats therefore allow energy to be stored in less than
half the body weight that would be required to store
the same amount of energy in carbohydrates
STRUCTURE OF TRIACYLGLYCEROLS

⦿ Triacylglycerols (fats)
contain three fatty
acids joined to
glycerol. In this
example, all three
fatty acids are
palmitate, but
triacylglycerols often
contain a mixture of
different fatty acids.
 LIPIDS
⦿ Phospholipids, the principal components of cell membranes,
consist of two fatty acids joined to a polar head group
⦿ In the glycerol phospholipids, the two fatty acids are bound to
carbon atoms in glycerol, as in triacylglycerols.
⦿ The third carbon of glycerol, however, is bound to a phosphate
group, which is in turn frequently attached to another small polar
molecule, such as choline, serine, inositol, or ethanolamine. 
⦿ Sphingomyelin, the only nonglycerol phospholipid in cell
membranes, contains two hydrocarbon chains linked to a polar
head group formed from serine rather than from glycerol.
⦿ All phospholipids have hydrophobic tails, consisting of the two
hydrocarbon chains, and hydrophilic head groups, consisting of the
phosphate group and its polar attachments.
⦿ Consequently, phospholipids are amphipathic molecules, part
water-soluble and part water-insoluble. This property of
phospholipids is the basis for the formation of biological
membranes
STRUCTURE OF PHOSPHOLIPIDS
 STRUCTURE OF PHOSPHOLIPIDS
⦿ Glycerol phospholipids contain two fatty acids joined
to glycerol.
⦿ The fatty acids may be different from each other and
are designated R1 and R2.
⦿ The third carbon of glycerol is joined to a phosphate
group (forming phosphatidic acid), which in turn is
frequently joined to another small polar molecule
(forming phosphatidylethanolamine,
phosphatidylcholine, phosphatidylserine, or
phosphatidylinositol).
⦿ In sphingomyelin, two hydrocarbon chains are bound
to a polar head group formed from serine instead of
glycerol.
 LIPIDS
⦿ In addition to phospholipids, many cell membranes
contain glycolipids and cholesterol.
⦿ Glycolipids consist of two hydrocarbon chains linked
to polar head groups that contain carbohydrates
⦿ They are thus similar to the phospholipids in their
general organization as amphipathic molecules.
⦿ Cholesterol, in contrast, consists of four hydrocarbon
rings rather than linear hydrocarbon chains
⦿ The hydrocarbon rings are strongly hydrophobic, but
the hydroxyl (OH) group attached to one end
of cholesterol is weakly hydrophilic, so cholesterol is
also amphipathic.
⦿ Two hydrocarbon chains are joined
to a polar head group formed from
serine and containing carbohydrates
(e.g., glucose).
CHOLESTEROL AND STEROID HORMONES

⦿ Cholesterol, an important component of cell membranes, is an amphipathic molecule because of

its polar hydroxyl group. Cholesterol is also a precursor to the steroid hormones, such
as testosterone and estradiol (a form of estrogen). The hydrogen atoms bonded to the ring
carbons are not shown in this figure.
 LIPIDS
⦿ In addition to their roles as components of cell
membranes, lipids function as signaling molecules,
both within and between cells.
⦿ The steroid hormones (such as estrogens
and testosterone) are derivatives of cholesterol
⦿ These hormones are a diverse group of chemical
messengers, all of which contain four hydrocarbon
rings to which distinct functional groups are
attached.
⦿ Derivatives of phospholipids also serve as messenger
molecules within cells, acting to convey signals from
cell surface receptors to intracellular targets
PROTEINS
 PROTEINS
⦿ While nucleic acids carry the genetic information of the cell, the
primary responsibility of proteins is to execute the tasks directed by
that information.
⦿ Proteins are the most diverse of all macromolecules, and each cell
contains several thousand different proteins, which perform a wide
variety of functions.
⦿ The roles of proteins include serving as structural components of cells
and tissues, acting in the transport and storage of small molecules
(e.g., the transport of oxygen by haemoglobin), transmitting
information between cells (e.g., protein hormones), and providing a
defense against infection (e.g., antibodies).
⦿ The most fundamental property of proteins, however, is their ability to
act as enzymes, catalyze nearly all the chemical reactions in biological
systems.
⦿ Thus, proteins direct virtually all activities of the cell.
⦿ The central importance of proteins in biological chemistry is indicated
by their name, which is derived from the Greek word proteios,
meaning “of the first rank.”
 PROTEINS
⦿ Proteins are polymers of 20 different amino
acids.
⦿ Each amino acid consists of a carbon atom
(called the α carbon) bonded to a carboxyl group
(COO-), an amino group (NH3+), a hydrogen
atom, and a distinctive side chain
⦿ The specific chemical properties of the different
amino acid side chains determine the roles of
each amino acid in protein structure and
function.
STRUCTURE OF AMINO ACIDS


⦿ Each amino acid consists of a central carbon atom (the α

carbon) bonded to a hydrogen atom, a carboxyl group,
an amino group, and a specific side chain (designated R).
⦿ At physiological pH, both the carboxyl and amino groups
are ionized
 PROTEINS
⦿ The amino acids can be grouped into four broad categories according to the properties of their
side chains
⦿ Ten amino acids have non-polar side chains that do not interact with water.
⦿ Glycine is the simplest amino acid, with a side chain consisting of only a hydrogen atom.
⦿ Alanine, valine, leucine, and isoleucine have hydrocarbon side chains consisting of up to four
carbon atoms.
⦿ The side chains of these amino acids are hydrophobic and therefore tend to be located in the
interior of proteins, where they are not in contact with water.
⦿ Proline similarly has a hydrocarbon side chain, but it is unique in that its side chain is bonded to
the nitrogen of the amino group as well as to the α carbon, forming a cyclic structure.
⦿ The side chains of two amino acids, cysteine and methionine, contain sulfur atoms.
⦿ Methionine is quite hydrophobic, but cysteine is less so because of its sulfhydryl (SH) group.
⦿ Sulfhydryl group of cysteine plays an important role in protein structure because disulfide bonds
can form between the side chains of different cysteine residues.
⦿ Finally, two non-polar amino acids, phenylalanine and tryptophan, have side chains containing
very hydrophobic aromatic rings.
AMINO ACIDS

⦿ The three-letter and one-letter abbreviations

for each amino acid are indicated.
⦿ The amino acids are grouped into four
categories according to the properties of
their side chains: non-polar, polar, basic, and
acidic.
 AMINO ACIDS
⦿ Five amino acids have uncharged but polar side chains - serine, threonine, and
tyrosine, which have hydroxyl groups on their side chains, as well as asparagine
and glutamine, which have polar amide (O=C—NH2) groups.
⦿ As the polar side chains of these amino acids can form hydrogen bonds with water,
these amino acids are hydrophilic and tend to be located on the outside
of proteins.
⦿ Lysine, arginine, and histidine have side chains with charged basic groups.
⦿ Lysine and arginine are very basic amino acids, and their side chains are positively
charged in the cell. They are very hydrophilic and are found in contact with water
on the surface of proteins.
⦿ Histidine can be either uncharged or positively charged at physiological pH, so it
frequently plays an active role in enzymatic reactions involving the exchange of
hydrogen ions.
⦿ Aspartic acid and glutamic acid, have acidic side chains terminating in carboxyl
groups. These amino acids are negatively charged within the cell and are therefore
frequently referred to as aspartate and glutamate. Like the basic amino acids,
these acidic amino acids are very hydrophilic and are usually located on the
surface of proteins.
 AMINO ACIDS
⦿ Amino acids are joined together by peptide
bonds between the α amino group of one amino acid and
the α carboxyl group of another
⦿ Polypeptides are linear chains of amino acids, usually
hundreds or thousands of amino acids in length.
⦿ Each polypeptide chain has two distinct ends, one
terminating in an α amino group (the amino, or N,
terminus) and the other in an α carboxyl group (the
carboxy, or C, terminus).
⦿ Polypeptides are synthesized from the amino to the
carboxy terminus, and the sequence of amino acids in a
polypeptide is written (by convention) in the same order.
FORMATION OF A PEPTIDE BOND


⦿ The carboxyl group of one amino acid is linked to the

amino group of a second.
 PROTEINS
⦿ The defining characteristic of proteins is that they are
polypeptides with specific amino acid sequences.
⦿ In 1953 Frederick Sanger was the first to determine the
complete amino acid sequence of a protein, the hormone
insulin.
⦿ Insulin was found to consist of two polypeptide chains,
joined by disulfide bonds between cysteine residues
⦿ Sanger's experiment revealed that each protein consists of a
specific amino acid sequence.
⦿ Proteins are currently sequenced using automated methods,
and the complete amino acid sequences of over 100,000
proteins are now known.
⦿ Each consists of a unique sequence of amino acids,
determined by the order of nucleotides in a gene
AMINO ACID SEQUENCE OF INSULIN

⦿ Insulin consists of two polypeptide chains, one of 21 and the other of 30

amino acids (indicated here by their one-letter codes).
⦿ The side chains of three pairs of cysteine residues are joined by disulfide
bonds, two of which connect the polypeptide chains.
 PROTEINS
⦿ The amino acid sequence of a protein is only the first element of
its structure.
⦿ Rather than being extended chains of amino acids, proteins adopt
distinct three-dimensional conformations that are critical to their
function.
⦿ These three-dimensional conformations of proteins are the result
of interactions between their constituent amino acids, so the
shapes of proteins are determined by their amino acid sequences.
⦿ This was first demonstrated by experiments of Christian Anfinsen
in which he disrupted the three-dimensional structures of proteins
by treatments, such as heating, that break noncovalent bonds—a
process called denaturation
⦿ Following incubation under milder conditions, such denatured
proteins often spontaneously returned to their native
conformations, indicating that these conformations were directly
determined by the amino acid sequence.
PROTEIN DENATURATION AND REFOLDING

⦿ Ribonuclease (RNase) is a protein of 124 amino acids (indicated by

numbers). The protein is normally folded into its native
conformation, which contains four disulfide bonds (indicated as
paired circles representing the cysteine residues).
 PROTEINS
⦿ 3D structure of proteins is most frequently analyzed by X-ray crystallography, a
high-resolution technique that can determine the arrangement of individual atoms
within a molecule.
⦿ A beam of X rays is directed at crystals of the protein to be analyzed, and the
pattern of X rays that pass through the protein crystal is detected on X-ray film.
As the X rays strike the crystal, they are scattered in characteristic patterns
determined by the arrangement of atoms in the molecule.
⦿ The structure of the molecule can therefore be deduced from the pattern of
scattered X rays (the diffraction pattern).
⦿ In 1958 John Kendrew was the first to determine the three-dimensional structure
of a protein, myoglobin—a relatively simple protein of 153 amino acids
⦿ Since then, the three-dimensional structures of several thousand proteins have
been analyzed.
⦿ Most, like myoglobin, are globular proteins with polypeptide chains folded into
compact structures, although some (such as the structural proteins of connective
tissues) are long fibrous molecules.
⦿ Analysis of the three-dimensional structures of these proteins has revealed several
basic principles that govern protein folding, although protein structure is so
complex that predicting the three-dimensional structure of a protein directly
from its amino acid sequence is impossible.
STRUCTURE OF MYOGLOBIN

⦿ Myoglobin is a protein
of 153 amino acids that
is involved in oxygen
transport.
⦿ The polypeptide chain
is folded around a
heme group that serves
as the oxygen-binding
site.
 PROTEIN STRUCTURE
⦿ Protein structure is generally described as having four levels.
⦿ The primary structure of a protein is the sequence of amino acids in
its polypeptide chain.
⦿ The secondary structure is the regular arrangement of amino acids
within localized regions of the polypeptide.
⦿ Two types of secondary structure, which were first proposed by Linus
Pauling and Robert Corey in 1951, are particularly common: the α
helix and the β sheet.
⦿ Both of these secondary structures are held together by hydrogen bonds
between the CO and NH groups of peptide bonds.
⦿ An α helix is formed when a region of a polypeptide chain coils around
itself, with the CO group of one peptide bond forming a hydrogen bond
with the NH group of a peptide bond located four residues downstream
in the linear polypeptide chain
⦿ In contrast, a β sheet is formed when two parts of a polypeptide chain
lie side by side with hydrogen bonds between them.
⦿ Such β sheets can be formed between several polypeptide strands,
which can be oriented either parallel or antiparallel to each other.
SECONDARY STRUCTURE OF PROTEINS

⦿ The most common types of secondary structure are the α helix and the β sheet. In an
α helix, hydrogen bonds form between CO and NH groups of peptide bonds separated
by four amino acid residues. In a β sheet, hydrogen bonds connect two parts of
a polypeptide chain lying side by side. The amino acid side chains are not shown.
TERTIARY STRUCTURE OF PROTEINS
⦿ Tertiary structure is the folding of
the polypeptide chain as a result of interactions
between the side chains of amino acids that lie in
different regions of the primary sequence
⦿ In most proteins, combinations of α helices and β
sheets, connected by loop regions of the polypeptide
chain, fold into compact globular structures
called domains, which are the basic units of tertiary
structure.
⦿ Small proteins, such as ribonuclease or myoglobin,
contain only a single domain; larger proteins may
contain a number of different domains, which are
frequently associated with distinct functions.
TERTIARY STRUCTURE OF RIBONUCLEASE
⦿ Regions of α-helix and
β-sheet secondary
structures, connected
by loop regions, are
folded into the native
conformation of the
protein. In this
schematic
representation of the
polypeptide chain as a
ribbon model, α
helices are
represented as spirals
and β sheets as wide
arrows.
 TERTIARY STRUCTURE OF PROTEINS
⦿ A critical determinant of tertiary structure is the localization
of hydrophobic amino acids in the interior of the protein and
of hydrophilic amino acids on the surface, where they interact with
water.
⦿ The interiors of folded proteins thus consist mainly of hydrophobic amino
acids arranged in α helices and β sheets; these secondary structures are
found in the hydrophobic cores of proteins because hydrogen bonding
neutralizes the polar character of the CO and NH groups of
the polypeptide backbone.
⦿ The loop regions connecting the elements of secondary structure are
found on the surface of folded proteins, where the polar components of
the peptide bonds form hydrogen bonds with water or with the polar side
chains of hydrophilic amino acids. Interactions between polar amino
acid side chains (hydrogen bonds and ionic bonds) on the protein surface
are also important determinants of tertiary structure.
⦿ In addition, the covalent disulfide bonds between the sulfhydryl groups of
cysteine residues stabilize the folded structures of many cell-surface or
secreted proteins.
QUARTERNARY STRUCTURE OF PROTEINS
⦿ The fourth level of protein structure, quaternary
structure, consists of the interactions between
different polypeptide chains in proteins composed
of more than one polypeptide.
⦿ Hemoglobin, for example, is composed of four
polypeptide chains held together by the same
types of interactions that maintain tertiary
structure 
QUATERNARY STRUCTURE OF HEMOGLOBIN

⦿ Hemoglobin is
composed of four
poly-peptide
chains, each of
which is bound to
a heme group.
The two α chains
and the two β
chains are
identical.
NUCLEIC ACIDS
NUCLEIC ACIDS 


Components of Nucleic Acids

Primary Structure of Nucleic Acids

49
NUCLEIC ACIDS
Nucleic acids are:
• molecules that store information for cellular
growth and reproduction.
• deoxyribonucleic acid (DNA) and ribonucleic acid
(RNA).
• large molecules consisting of long chains of
monomers called nucleotides.

50
NUCLEIC ACIDS

The nucleic acids DNA and RNA

consist of monomers called
nucleotides that consist of a
• pentose sugar.
nucleotide
• nitrogen-containing base.
• phosphate.

51
NITROGEN BASES
The nitrogen bases in
DNA and RNA are
• pyrimidines C, T, and
U.
• purines A and G.

52
NITROGEN-CONTAINING BASES IN DNA AND
RNA
DNA contains the nitrogen bases
• Cytosine (C)
• Guanine (G) same in both DNA and RNA
• Adenine (A)
• Thymine (T) different in DNA than RNA
RNA contains the nitrogen bases
• Cytosine (C)
• Guanine (G) same in both DNA and RNA
• Adenine (A)
• Uracil (U) different in DNA than RNA

53
PENTOSE SUGARS
The pentose (five-carbon) sugar
• in RNA is ribose.
• in DNA is deoxyribose with no O atom on carbon 2’.
• has carbon atoms numbered with primes to
distinguish them from the atoms in nitrogen bases.

54
NUCLEOSIDES
A nucleoside
• has a nitrogen base linked
by a glycosidic bond to
C1’ of a sugar (ribose or
deoxyribose). HO
• is named by changing the
nitrogen base ending to -
osine for purines and
–idine for pyrimidines.

55
NUCLEOTIDES
A nucleotide
• is a nucleoside that
forms a phosphate
ester with the C5’ –OH
group of a sugar (ribose
or deoxyribose).
• is named using the
name of the nucleoside
followed by
5’-monophosphate.

56
FORMATION OF A NUCLEOTIDE
A nucleotide forms when the −OH on C5’ of a
sugar bonds to phosphoric acid.
NH2 NH2

N N

O 5’ O O 5’ O N
N
O- P OH + HO CH2 O- P O CH2
O O
-
O- O

OH OH

deoxycytidine and phosphate deoxycytidine monophosphate (dCMP)

57
NUCLEOSIDES AND NUCLEOTIDES
WITH PURINES

58
NUCLEOSIDES AND NUCLEOTIDES
WITH PYRIMIDINES

59
NAMES OF NUCLEOSIDES AND
NUCLEOTIDES

61
LEARNING CHECK
Give the name and abbreviation for the following
and list its nitrogen base and sugar.

62
SOLUTION
Guanosine 5’-monophosphate (GMP)
nitrogen base: guanine
sugar: ribose

63
PRIMARY STRUCTURE OF NUCLEIC
ACIDS
In the primary structure of nucleic acids

• nucleotides are joined by phosphodiester

bonds.

• the 3’-OH group of the sugar in one nucleotide

forms an ester bond to the phosphate group on
the 5’-carbon of the sugar of the next
nucleotide.

64
PRIMARY STRUCTURE OF NUCLEIC
ACIDS

65
STRUCTURE OF NUCLEIC ACIDS
A nucleic acid
• has a free 5’-phosphate
group at one end and a
free 3’-OH group at the
other end.
• is read from the free 5’-
end using the letters of
the bases.
• This example reads
—A—C—G—T—.

66
EXAMPLE OF RNA STRUCTURE
The primary structure
of RNA,
• is a single strand of
nucleotides with
bases A, C, G, and
U.
• is linked by
phosophodiester
bonds between
ribose and
phosphate.

Copyright © 2005 by Pearson Education, Inc.

Publishing as Benjamin Cummings

67
EXAMPLE OF DNA
In DNA,
• nucleotides
containing
bases A, C, G,
and T are
linked by ester
bonds between
deoxyribose
sugars and
phosphate
groups.
Copyright © 2005 by Pearson Education, Inc.
Publishing as Benjamin Cummings

68
DNA DOUBLE HELIX
A double helix
• is the structure of DNA.
• has two strands of nucleotides that wind
together.
• is held in place by of two hydrogen bonds that
form between the base pairs A-T.
• is held in place by three hydrogen bonds that
form between the base pairs G-C.

69
Nucleic Acids
RNA
Each nucleotide has three parts
A five-carbon sugar – ribose
A nitrogenous base (having N in the ring structure of the
molecule)
A phosphate group
Nucleic Acids
RNA
During the assembly of the
nucleic acid strand
The OH group on the
3’ carbon of ribose
on one nucleotide is
linked by an ester
bond to the
phosphate group of
its neighbor
The nucleotides are
connected by sugar-
phosphate linkages
NUCLEIC ACIDS


Nucleotides not involved in building nucleic acids

Adenosine triphosphate (ATP) – energy storage
Guanosine triphosphate (GTP) – signal cascade
COMPLEMENTARY BASE PAIRS
DNA contains complementary base pairs in which
• Adenine is always linked by two hydrogen bonds
with thymine (A−T).
• Guanine is always linked by three hydrogen with
Cytosine (G−C).

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DOUBLE HELIX OF DNA
In the double helix of DNA
• two strands of
nucleotides form a
double helix structure
like a spiral stair case.
• hydrogen bonds link
bases A–T and G–C.
• the bases along one
strand complement the
bases along the other.
Copyright © 2005 by Pearson Education, Inc.
Publishing as Benjamin Cummings

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C1 Nucleic Acid Structure
DNA double helix
•Watson and Crick , 1953. Essential for replicating DNA and transcribing RNA
•Two separate strands
Antiparellel (5’→3’ direction)
Complementary (sequence)
Base pairing: hydrogen
bonding that holds two
strands together

• Sugar-phosphate backbones
(negatively charged): outside
• Planar bases (stack one
above the other): inside
C1 Nucleic Acid Structure

•Double helix
•B form:
Right-handed
10 base pairs/turn
34 Å /turn
Diameter: ca. 20 Å

Other forms:
A: 11 bases/turn, base
plate 20° slant
Z: 12 bases/turn, left-
handed helical, one
groove
LEARNING CHECK
Write the complementary base sequence for the
matching strand in the following DNA section:

—A—G—T—C—C—A—A—T—C—

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SOLUTION
Write the complementary base sequence for the
matching strand in the following DNA section:

—A—G—T—C—C—A—A—T—C—

’—T—C—A—G—G—T—T—A—G—

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