Protein, RNA and DNA are made up of smaller building blocks. Protein is made from amino acids that are linked through peptide bonds. RNA and DNA are made from nucleotides that contain a phosphate group, a sugar (ribose in RNA and deoxyribose in DNA), and a nitrogenous base. There are four levels of protein structure - primary, secondary, tertiary and quaternary. RNA and DNA store and transmit genetic information through their structures and functions such as replication, transcription and translation.

1. PROTEIN, RNA AND
DNA
MADE BY ILYES REKIK,SADDAH ELMAHDI, ABDULRAHMAN ELSAKA

2. PROTEIN
Keyword
1. Peptide bond:amide linkage
2. Amino acids sequence:the
unique order of amino acids
chain
3. Amino:N-terminus
4. Carboxylic acid :C-terminus
5. Folding :different distinct
side chain
● Large molecules that is built by amino acid(with different properties)
● Protein carbon chain it consists of amino group(NH),carboxylic(COOH)
and side chain
● Amino acid are linked by peptide covalent bond in amino acids sequence
● Amino acids have two different end amino and carboxylic
● Flexibility is directly proposed to length of chain
● Protein have 4 types of folding(primary,secondary,tertiary,quaternary)
● Examples of forms of protein(hemoglobin,DNA,
Catalase,myoglobin,insulin,collagen,porin,lysozyme)
● By examining the the structure of smaller protein domain we illustrate
protein conformation

3. Keyword
1. Denatured: unfold of protein
2. Renatures:refolds spontaneously
Folding
● The non “covalent bond”(van der waals, hydrogen,electrostatic)it is
fold to a particularly stable three-dimensional shape
● Protein folding could be aided by hydrophobic forces
● Polar amino acid tend to fall outside so they can interact, non polar
fall inside so they form hydrophobic force that are hidden from water
● More non-covalent bonds attached together it gives strong bond
● Protein can be unfolded by solvents that disrupt so it convert protein
into flexible polypeptide so it lose natural shape, after denaturing
solvent is removed protein will return to its normal form

4. ● Protein normal folds to single conformation, this conformation if
it changes in shape it change the protein function
● Incorrect folding it can damage the cell or tissue
● Al zheimer ,Huntington disease, prion disease(animal), Jacob
disease
● Prion protein can change the normal protein to incorrect folding
protein
Protein can fold to its correct conformation without any external help
and this is assisted by protein called molecular chaperones “bind to
partly folded chains and let them fold”.i
Incorrect Folding

5. Protein structure

6. THE FOUR LEVEL OF PROTEIN STRUCTURE
● The simplest level of protein structure, primary structure, is simply the sequence of
amino acids in a polypeptide chain.
● The next level of protein structure, secondary structure, refers to local folded structures
that form within a polypeptide due to interactions between atoms of the backbone.
● The overall three-dimensional structure of a polypeptide is called tertiary structure of
the protein.
● Several polypeptide chains, also referred to as subunits, make up some proteins. These
individual components combine to form : quaternary structure of the protein.

7. Primary structure
● A structure of a biological molecule in which there is a precise sequence or order of monomeric units. It
serves as the covalent backbone of biological molecules (such as DNA and proteins).
● The primary structure is comprised of a linear chain of amino acids,
● The primary structure of a protein — its amino acid sequence — drives the folding and intramolecular
bonding of the linear amino acid chain, which ultimately determines the protein's unique three-dimensional
shape.

8. Secondary structure
● The most common types of secondary structures are the α helix
and the β pleated sheet. Both structures are held in shape by
hydrogen bonds, which form between the carbonyl O of one amino
acid and the amino H of another.
● In an α helix, the carbonyl (C=O) of one amino acid is hydrogen
bonded to the amino H (N-H) of an amino acid that is four down the
chain.
● In a β pleated sheet, two or more segments of a polypeptide chain
line up next to each other, forming a sheet-like structure held
together by hydrogen bonds.

9. Tertiary structure
● At this level, every protein has a specific three-dimensional shape and
presents functional groups on its outer surface, allowing it to interact
with other molecules, and giving it its unique function.
● The tertiary structure is primarily due to interactions between the R
groups of the amino acids that make up the protein.
● It is generally stabilized by outside polar hydrophilic hydrogen and
ionic bond interactions, and internal hydrophobic interactions between
nonpolar amino acid side chains.

10. Quaternary structure
● The quaternary structure of a protein is the association of several protein chains or subunits
into a closely packed arrangement.
● The quaternary structure refers to the number and arrangement of the protein subunits with
respect to one another. Examples of proteins with quaternary structure include hemoglobin, DNA
polymerase, ribosomes, antibodies, and ion channels.
● In general, the same types of interactions that contribute to tertiary structure (mostly weak
interactions, such as hydrogen bonding and London dispersion forces) also hold the subunits
together to give quaternary structure.

12. All Proteins Bind To Other Molecules
● The properties of the protein molecule depend on its interaction with other molecules.
For instance, an antibody can attach to a bacteria or virus to destroy them, while an
enzyme called hexokinase can catalyze a reaction between two molecules by binding
glucose and ATP.
● All types of proteins can bind to other molecules. In some cases, the binding is very tight,
while in others, it is weak or short-lived. Despite this, the specificity of the protein's
binding is very high, as it can easily bind just a one or even a few molecules out of
thousands that it encounters.

13. Antibody Binding Site
An antibody is a protein produced by your immune system to attack and fight off these antigens. Each
antibody consists of four polypeptides– two identical heavy chains and two identical light chains joined to
form a "Y" shaped molecule.

14. Enzymes Are Powerful and Highly Specific Catalysts
● Some proteins can perform their functions by binding to another substance. For instance, an actin
molecule can only bind to its own molecules to form a filament. However, other proteins, such as those
that are involved in the production of enzymes, require a different type of binding to perform their
functions and it is ligand.
● A ligand is a small molecule that is able to bind to proteins by weak interactions such as ionic bonds,
hydrogen bonds, Van der Waals interactions, and hydrophobic effects
● The catalytic actions of enzymes are remarkable, as they determine the chemical transformations that
occur in cells when they bind to certain types of substrates. They then convert these substrates into
chemical-modified products. Enzymes typically perform these actions in a matter of a millionths of a
second, and they allow cells to break or make covalent bonds in a controlled manner..

15. NUCLEIC ACID
● Large molecules that is built by aminoacid(with different properties)
● Protein carbon chainit consistsof amino group(nh2),carboxylic(cooh)andside chain
ILYES REKIK PART

16. DNA, abbreviation of deoxyribonucleic acid :is the molecule that
carries genetic information for the development and functioning of
an organism
● DNA is made of two linked strands that wind around each
other to resemble a twisted ladder — a shape known as a
double helix
Location:
In eukaryotic cells, the DNA
is located inside the nucleus
on the chromosomes.
Functions
● Replication.
● Gene expression.
● Mutation.
● Transcription.
● Translation.
DNA

17. NUCLEIC ACID
● The monomers of nucleic acids is nucleotide
● There is two types of nucleic acid
○ Deoxyribonucleic acid(DNA)
○ Ribonucleic acid(RNA)
● Subunits of DNA and RNA- nucleotides
○ Phosphate group
○ Sugar
○ Nitrogenous base

18. RNA VS DNA
● RNA shares Adenine (‘A’),
Guanine (‘G’) and Cytosine
(‘C’) with DNA, but contains
Uracil (‘U’) rather than
Thymine
● RNA only has one strand
● contains deoxyribose sugar
● The bases in DNA are
Adenine (‘A’), Thymine (‘T’),
Guanine (‘G’) and Cytosine
(‘C’).
● DNA consists of two strands,
arranged in a double helix
● DNA contains the
Deoxyribosem sugar

19. RNA VS DNA
● RNA, containing a ribose
sugar, is more reactive than
DNA and is not stable in
alkaline conditions
● RNA forms in the nucleolus,
and then moves to
specialised regions of the
cytoplasm depending on the
type of RNA formed
● Due to its deoxyribose sugar,
which contains one less
oxygen-containing hydroxyl
group, DNA is a more stable
molecule than RNA,
● DNA is found in the nucleus,
with a small amount of DNA
also present in mitochondria.

20. Bases
Pyrimidine
purine
Cytosine
uracil
adenine
guanine
thymine

21. Sugars
Ribose
Deoxyribose
Contains:OH,H
Deoxyribonucleic
acid(DNA)
Contains:OH,OH
Ribonucleic
acid(RNA)
Pentose

22. Phosphates
● They normally join in C5 hydroxyl group in deoxyribose or ribose sugar
● Most common phosphate groups are dimonophopshate ,triphosphate
● Phosphate makes nucleotide negatively charged

23. Nomenclature
● Nucleoside is a nitrogenous base that bound to a pentose
sugar (ribose or deoxyribose)
● Nucleotide :Nucleoside is a nitrogenous base that bound to a
pentose sugar (ribose or deoxyribose) and phosphate group
● In naming both nucleoside and nucleotide we start with the
sugar
● Then we go to the nucleoside it self and if phosphate group is
present we go for it after nucleoside
● Basically (sugar)+(nucleoside)+(phosphate)
● Thymine bond only with
deoxyribose sugar

24. Nomenclature
Examples (nucleotides)

25. Nomenclature
Examples (nucleosides)

26. Another functions Nucleotides
Energy
They carry chemical energy in their easily
hydrolyzed phosphoanhydride bonds.
● Like ATP,ADP,etc
Metabolic
regulators
They combine with other groups to form
coenzymes.
● coenzymes like NAD and NADP
Signaling
They are used as signaling molecules in
the cell.
● cyclic AMP (cAMP), a messenger molecule
which regulate metabolism and transport chemical
signals to cells.
which come from ADP

27. Nucleotides to
nucleic acid
● Nucleotides are joined together forming nucleic acids
● Nucleotide join other nucleotide by linking its
phosphate group which located in the fifth
carbon atom in a deoxyribose sugar with with
Third carbon atom in a deoxyribose sugar in the
Other nucleotide
● They are joined together in formation which create
phosphodiester linkage

28. References(nucleic acid)
● General Data Protection Regulation(GDPR) Guidelines BYJU’S. (2021, March 22). BYJUS. Retrieved October 19, 2022,
from https://byjus.com/biology/difference-between-purines-and-pyrimidines/
● Deoxyribonucleic Acid (DNA). (n.d.). Genome.gov. Retrieved October 19, 2022, from https://www.genome.gov/genetics-
glossary/Deoxyribonucleic-Acid
● BD Editors. (2019, October 4). Nucleotide. Biology Dictionary. Retrieved October 19, 2022, from
https://biologydictionary.net/nucleotide/
● Lecture 3
● Replication. (n.d.). Genomics. Retrieved October 19, 2022, from
https://serc.carleton.edu/microbelife/research_methods/genomics/replication.html