PROTEIN Amino acids are attached to other amino acids by

covalent bonds, known as PEPTIDE BOND, which are

Protein – are one of the most abundant organic formed by dehydration synthesis reactions.
molecules in living systems and have the most diverse
range of functions of all macromolecules. They are all, Protein Structure – the structure of a protein is critical
however, polymers of amino acids, arranged in a linear to its function.
sequence.
 Primary Structure – the unique sequence of
Types and Function of Proteins amino acids in a polypeptide chain.
 Secondary Structure – the local folding of the
Enzymes – are produced by living cells, are catalysts in
polypeptide in some regions gives rise to the
biochemical reaction (like digestion) and are usually
secondary structure of the protein.
complex or conjugated proteins. They may help in
 Tertiary Structure – the unique three-dimensional
breakdown, rearrangement, or synthesis reaction.
structure of a polypeptide.
Enzymes are proteins that catalyze biochemical
 Quaternary Structure – protein consisting of
reactions.
more than one polypeptide.
 Catabolic Enzyme – enzymes that break down
Denaturation – often reversible, allowing the protein to
their substrates.
resume its function.
 Anabolic Enzyme – those that build more
complex molecules from their substrates. Protein Folding – correct folding of proteins is critical
 Catalytic Enzyme – enzymes that affect the rate of to their function.
reaction.
In all these reactions, an enzyme will bind with the
substrate (reactant molecule) in an area on the enzymes
surface called active site, forming a substrate-enzyme
complex.
It should be noted that all enzymes increase the rate of
reaction and, therefore, are considered to be organic
catalysts.
Temperature – generally, chemical reactions increase
as temperature increases because the reacting
molecules move faster and collide more often.
pH – indicates the acidity/basicity of a solution.
Measures the concentration of hydrogen ions (H+). The
lower the pH, the higher the concentration of H+ ions
there is.
Substrate Concentration – if enzyme concentration
remains constant, enzyme activity increases as substrate
concentration increases, but only as long as there are
active sites available.
Amino Acid – are the monomers that make up proteins.
All proteins are made up of different arrangements of the
same 20 amino acids.
NUCLEIC ACIDS
What are nucleic acids?
Polypeptides – technically a polymer of amino acids,
whereas the term protein is a polypeptide or  Nucleic acids are the most important
polypeptides that have a distinct shape and a unique macromolecules for the continuity of life. They
function.
 carry genetic blueprint of a cell and carry
instructions for the functioning of the cell.
Two main types of nucleic acids:
1. Deoxyribonucleic acid (DNA)
2. Ribonucleic acid (RNA)
1. Deoxyribonucleic acid (DNA)
 DNA is 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
membranous envelope.
 In eukaryotic cells, but not in prokaryotes, DNA
forms a complex with histone proteins to form
chromatin, the substance of eukaryotic
chromosomes.
 DNA controls all of the cellular activities by
turning the genes “on” or “off”.
2. Ribonucleic acid (RNA)
 Is mostly involved in protein synthesis. The
DNA molecules never leave the nucleus, but use
an intermediary to communicate with the rest of
the cell instead. This intermediary is the
messenger RNA (mRNA).
 Other types of RNA - like rRNA, tRNA, and
microRNA - are involved in protein synthesis
and its regulation.
DNA and RNA
 They are made up of monomers known as
nucleotides.
 The nucleotides combine with each other form a
polynucleotide.
Three Components of Nucleotide:
1. Nitrogenous Base
2. Pentose Sugar
3. Phosphate Groups
Nitrogenous Base
 Each nitrogenous base in a nucleotide is attached
to a sugar molecule, which is attached to one or
more phosphate groups.
 Important components of nucleotides that are
organic molecules that contain carbon and
nitrogen.
 They are bases because they contain an amino
group that has the potential of binding an extra
hydrogen, thus, decreasing the hydrogen ion
concentration in its environment and making it
more basic.
Each nucleotide in DNA contains one of four possible
nitrogenous bases:
1. Adenine (A)
2. Guanine (G)
3. Cytosine (C)
4. Thymine (T)
Purines
 Adenine and guanine are classified as purines.
 The primary structure of a purine is two carbon-
nitrogen rings represented by adenine and
guanine.
Pyrimidines
 Cytosine, thymine, and uracil (RNA) on the
other hand, are classified as pyrimidines which
have a single carbon-nitrogen ring as their
primary structure.
Pentose Sugar
 The pentose sugar in DNA is deoxyribose, and
in RNA, the sugar is ribose.
 The carbon atoms of the sugar molecule are
numbered as 1, 2, 3', 4', and 5’ (1' is read as
"one prime").
REMEMBER!
 In molecular biology shorthand, the nitrogenous
bases are simply known by their symbols: A, T,
G, C, & U.
 DNA contains A, T, G, & C.
 RNA contains A, U, G, & C.
DNA Double-Helix Structure
 The sugar and phosphate lie on the outside of the
helix, forming the backbone of the DNA. The
nitrogenous bases are stacked in the interior, like
the steps of a staircase, in pair; the pairs are
bound to each other by hydrogen bonds.
 This is referred to as antiparallel orientation
and is important to DNA replication and in many
nucleic acid interactions.
Chargaff’s Rule  The smallest RNA molecules, and their role
involves the regulation of gene expression by
 Only certain types of base pairing are allowed;
interfering with the expression of certain mRNA
for example, a certain purine can only pair
messages.
with a certain pyrimidine. This means A can
pair with T, and G can pair with C. This is Central Dogma of Life
known as the base complementary rule or
Chargaff's Rule.  DNA dictates the structure of mRNA in a
process known as transcription.
4 Major Types of RNA  RNA dictates the structure of protein in a
process known as translation.
1. Messenger RNA (mRNA)
 This is known as the Central Dogma of Life,
2. Ribosomal RNA (rRNA)
3. Transfer RNA (tRNA) which holds true for all organisms; however,
4. Micro RNA (miRNA) exceptions to the rule occur in connection with
viral infections.
Messenger RNA (mRNA)

 Carries the message from DNA, which

controls all of the cellular activities in a cell.
 If a cell requires a certain protein to be
synthesized, the gene for this product is turned
"on" and the messenger RNA is synthesized in
the nucleus.
 The mRNA is read in sets of three bases knows
as codons. Each codon codes for a single amino
acid.
 In this way, the mRNA is read and the protein
product is made. In the cytoplasm, the mRNA
interacts with ribosomes and other cellular
machinery.
Ribosomal RNA (rRNA)

 Ribosomal RNA (rRNA) is a major constituent

of ribosomes on which the mRNA binds.
 The rRNA ensures the proper alignment of the
mRNA and the ribosomes
 The rRNA of the ribosome also has an
enzymatic activity (peptidyl transferase) and
catalyzes the formation of the peptide bonds
between two aligned amino acids.
Transfer RNA (tRNA)

 Transfer RNA (tRNA) is one of the smallest of

the four types of RNA, usually 70-90 nucleotides
long.
 It carries the correct amino acid to the site of
protein synthesis.
 It is the base pairing between the tRNA and
mRNA that allows for the correct amino acid to
be inserted in the polypeptide chain.
Micro RNA (miRNA)