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Organic Molecules
• process in which
polymers are broken
down into monomers by
breaking its covalent
bonds.
Macromolecules
• Carbohydrates
• Lipids
• Proteins
• Nucleic Acids
Carbohydrates
• organic molecules that
consist of carbon,
hydrogen, and oxygen.
• (CH2O)n : often in the
proportion 1:2:1
• Types:
– Monosaccharides
– Disaccharides
– Polysaccharides
Monosaccharides
• simple sugars
• number of carbon ranges from 3-7.
• mostly end its name with the suffix -ose.
– with aldehyde group (aldose)
– with ketone group (ketose)
– with different numbers of carbon (triose, pentose,
etc.)
• Examples:
– glucose, galactose, fructose ( C6H12O6)
Disaccharides
• Common Disaccharides:
– Lactose
– Maltose
– Sucrose
Disaccharides: Hydrolysis
Polysaccharides
• it contains fused
ring systems
consisting of three
six-membrane rings
and one five-
membrane rings.
• is an important part
of many hormones.
Protein
• a biomolecule composed of
C, H, O, and N.
• is the most abundant organic
molecule in living systems
and has the most diverse
range of functions of all
macromolecules.
• it may be structural,
regulatory, contractile,
protective, storage, for
transport membrane,
enzymes.
– amino acids - monomers
of protein.
Amino Acids
2. Regulatory or Signal
Protein (Hormones) - are
chemical signaling
molecules, usually small
proteins or steroids,
secreted by the
endocrine cells that act
to control or regulate
specific physiological
processes, including
growth, development,
metabolism, and
reproduction.
Types of Protein
• Structural Protein - proteins that form the structural partof
cells and tissues.
Types of Protein
• Contractile Proteins -
are in the form of
actin and myosin,
which are found in
cells to allow
movement and cause
muscle contraction.
Types of Protein
• Storage Protein - serves as reserves of amino acids, which can
be used later on to nourish the growth and development of
organisms.
– prevalent in seeds, egg white, milk
Protein Structure
• Primary Structure -
refers to the linear
polypeptide chain,
which does not
achieve any folding
state.
• Ex: Insulin
Protein Structure
• Secondary Structure - refers
to the interaction of the
hydrogen bond donor and
acceptor residues of the
repeating peptide unit.
– the two most important
secondary structures of
proteins, the alpha helix
and the beta sheet.
– Ex: Myoglobin
Protein Structure
• is made up of:
– Five-carbon sugar
– Phosphate group
– Nitrogenous bases
• Purines (double ringed) - Guanine (G) and
Adenine (A)
• Pyrimidines (single-ringed) - Cytosine (C),
Thymine (T), & Uracil (U)
Nucleotide
Nitrogenous Bases
Properties of DNA
• double helix
• has complementary
bases of A-T; C-G
• deoxyribose sugar
Properties of RNA
• has complementary
bases G-C; A-U
• ribose sugar
• single-stranded
Types of RNA
• mRNA
• tRNA
• rRNA
• Regulatory RNA
mRNA
• is an intermediate between a
protein-coding gene and its
protein product.
• If a cell needs to make a
particular protein, the gene
encoding the protein will be
turned “on,” meaning an
RNA-polymerizing enzyme
will come and make an
RNA copy, or transcript, of
the gene’s DNA sequence.
• The transcript carries the
same information as the
DNA sequence of its gene.
Regulatory RNA