MOLECULAR

STRUCUTURE OF DNA,
DASAL – AZAGRA - LOBO

RNA & PROTEINS

WHAT IS DNA?
Deoxyribonucleic acid is a molecule
composed of two chains that coil around
each other to form a double helix carrying
genetic instructions for the development,
functioning, growth and reproduction of all
known organisms and many viruses.
Deoxyribonucleic acid, or DNA, contains
the instructions an organism needs to
develop, live and reproduce. These
instructions are found inside every cell,
and are passed down from parents to
their children.

Thus, the DNA is called as the blueprint

of life.
Deoxyribonucleic acid, or DNA, contains
the instructions an organism needs to
develop, live and reproduce. These
instructions are found inside every cell,
and are passed down from parents to
their children.

Thus, the DNA is called as the blueprint

of life.
Short History of DNA: Discovery of the DNA
double helix

1928 1952 1953

Frederick Griffith Rosalind Franklin Watson & Crick

• Discovers that a factor • X-ray of DNA • Described the DNA
in diseased bacteria can Molecule from
transform harmless Franklin’s X-ray
bacteria into deadly
bacteria
FIRST XRAY OF DNA
Watson & Crick proposed that…

• The DNA had a specific pairing between the nitrogenous bases.

ADENINE ---- THYMINE
CYTOSINE ---- GUANINE

• DNA was made of 2 long strands of nucleotides arranged in a specific

way called the “Complementary Rule”.
DNA Structure
DNA is made up of molecules called
nucleotides.

Each nucleotide contains a

phosphate group, a sugar group and a
nitrogen base.
NITROGENOUS BASES OF DNA
There are four nitrogenous
bases:
Purine Bases:
• Adenine (A)
• Guanine (F)
Pyrimidine Bases:
• Cytosine (C)
• Thymine (T)
Chargaff’s Rule
• Adenine must pair with Thymine
• Guanine must pair with Cytosine
• Their amounts in a given DNA molecules will be about the same
WHAT IS RNA?
Ribonucleic acid is a polymeric
molecule essential in various
biological roles in coding, decoding,
regulation and expression of
genes. The main function of RNA is
to carry information of amino acid
sequence from the genes to where
proteins are assembled on ribosomes
in the cytoplasm.
RNA STRUCTURE
RNA is typically single stranded
and is made of ribonucleotides that
are linked by phosphodiester
bonds. A ribonucleotide in the
RNA chain contains ribose (the
pentose sugar), one of the four
nitrogenous bases (A, U, G, and
C), and a phosphate group.
NITROGENOUS BASES OF RNA
There are four
nitrogenous bases:
Purine Bases:
• Adenine (A)
• Guanine (F)
Pyrimidine Bases:
• Cytosine (C)
• Uracil (U)
Types of RNA
mRNA tRNA rRNA
“messenger” “transfer” “ribosomal”
Made using DNA Transfers an amino acid to the Makes up the bulk of ribosomes
growing protein
Carries genetic information
from the nucleus to the Cloverleaf shape
ribosome
Every 3 bases (codon) specified 3 complimentary bases
(anticodon) binds to the mRNA
an amino acid codon
 DNA VS. RNA
DNA RNA
Double-Stranded Single-Stranded
Has Thymine as a base Has Uracil as a base
Deoxyribose as the sugar Ribose as the sugar
Maintains protein-encoding Uses protein-encoding
information information
 WHAT IS PROTEIN?
Proteins are any of a class of
nitrogenous organic compounds that
consist of large molecules composed of
one or more long chains of amino acids
and are an essential part of all living
organisms, especially as structural
components of body tissues such as
Protein Structure muscle, hair, collagen, etc., and as
enzymes and antibodies.
WHAT IS PROTEIN?
Proteins do most of the work in cells
and are required for
the structure, function, and
regulation of the body's tissues and
organs. Proteins are made up of
hundreds or thousands of smaller
units called amino acids, which are
attached to one another in long
chains.
AMINO ACIDS
Amino acids are organic compounds
that combine to form proteins. 

Amino acids and proteins are the

building blocks of life.
AMINO ACIDS
ESSENTIAL AMINO ACIDS NON ESSENTIAL AMINO
ACIDS
1. Histidine 1. Alanine,
2. Isoleucine 2. Arginine
3. Leucine 3. Asparagine
4. Lysine 4. Aspartic acid
5. Methionine 5. Cysteine
6. Phenylalanine 6. Glutamic acid
7. Threonine 7. Glutamine
8. Tryptophan 8. Glycine
9. Valine 9. Proline
10.Serine
11.Tyrosine
Four Levels of Protein Structure

1. Primary Structure
2. Secondary Structure
3. Tertiary Structure
4. Quaternary Structure
Primary Structure
Primary Structure describes the unique order in which amino acids are
linked together to form a protein. Proteins are constructed from a set of
20 amino acids. Generally, amino acids have the following structural
properties:
A carbon (the alpha carbon) bonded to the four groups below:
• A hydrogen atom (H)
• A Carboxyl group (-COOH)
• An Amino group (-NH2)
• A "variable" group or "R" group
All amino acids have the alpha carbon bonded to a hydrogen atom,
carboxyl group, and an amino group. The "R" group varies
among amino acids and determines the differences between
these protein monomers. The amino acid sequence of a protein is
determined by the information found in the cellular genetic code. The
order of amino acids in a polypeptide chain is unique and specific to a
particular protein. Altering a single amino acid causes a gene mutation,
which most often results in a non-functioning protein.
Secondary Structure
Secondary Structure refers to the coiling or folding of a polypeptide
chain that gives the protein its 3-D shape. There are two types of
secondary structures observed in proteins. One type is the alpha (α)
helix structure. This structure resembles a coiled spring and is secured
by hydrogen bonding in the polypeptide chain. The second type of
secondary structure in proteins is the beta (β) pleated sheet. This
structure appears to be folded or pleated and is held together by
hydrogen bonding between polypeptide units of the folded chain that lie
adjacent to one another.
Tertiary Structure
Tertiary Structure refers to the comprehensive 3-D structure of the
polypeptide chain of a protein. There are several types of bonds and
forces that hold a protein in its tertiary structure. 
• Hydrophobic interactions greatly contribute to the folding and
shaping of a protein. The "R" group of the amino acid is either
hydrophobic or hydrophilic. The amino acids with hydrophilic "R"
groups will seek contact with their aqueous environment, while amino
acids with hydrophobic "R" groups will seek to avoid water and
position themselves towards the center of the protein. ​
• Hydrogen bonding in the polypeptide chain and between amino acid
"R" groups helps to stabilize protein structure by holding the protein in
the shape established by the hydrophobic interactions.
• Due to protein folding, ionic bonding can occur between the
positively and negatively charged "R" groups that come in close
contact with one another.
• Folding can also result in covalent bonding between the "R" groups of
cysteine amino acids. This type of bonding forms what is called
a disulfide bridge. Interactions called van der Waals forces also assist
in the stabilization of protein structure. These interactions pertain to
the attractive and repulsive forces that occur between molecules that
become polarized. These forces contribute to the bonding that occurs
between molecules.
Quaternary Structure
Quaternary Structure refers to the structure of a protein
macromolecule formed by interactions between multiple polypeptide
chains. Each polypeptide chain is referred to as a subunit. Proteins with
quaternary structure may consist of more than one of the same type of
protein subunit. They may also be composed of different subunits.
Hemoglobin is an example of a protein with quaternary structure.
Hemoglobin, found in the blood, is an iron-containing protein that binds
oxygen molecules. It contains four subunits: two alpha subunits and two
beta subunits.