BIOMOLECULE

CARBON IS THE CENTRAL

ELEMENT

All biomolecules contain a Carbon chain or ring

Carbon has 4 outer shell electrons (valence = 4)

Therefore its bonding capacity is great

It forms covalent bonds hence, has strong

bonds

Once bound to other elements (or to other

Carbons), it is very stable

CARBON LINKAGES

Single chains
Rings

CARBON BINDS TO MORE

THAN JUST HYDROGEN

To OH groups in sugars
To NH2 groups in amino acids
To H2PO4 groups of
nucleotides of DNA, RNA,
and ATP

OH, NH2, PO4 are called functional groups!

Functional
groups

SAME MOLECULAR
FORMULAS BUT
DIFFERENT STRUCTURES

Structural isomer = difference in the C

skeleton structure
Stereoisomer = difference in location of
functional groups

ENANTIOMERS ARE
SPECIAL TYPES OF
STEREOISOMERS
Enantiomers are mirror
images
of each other
-One such enantiomer
contains
C bound to 4 different
molecules and
is called a chiral molecule
-Chiral molecules rotate
polarized light to the right
(D form) or to the left
(L form) molecules

MONOMERS AND POLYMERS

Monomers are made into polymers via dehydration reactions

Polymers are broken down into monomers via hydrolysis
reactions

CARBOHYDRATES

CARBOHYDRATES

Simple sugars
(monosaccharides)
Only one 3-C, 5-C,
6-C chain or ring
involved

Examples of sugar monomers

CARBOHYDRATES

Double sugars
(disaccharides)
Two 6-C chains or
rings bonded
together

CARBOHYDRATES

Complex carbos
(polysaccharides)
Starch
Cellulose
Glycogen
Chitin

Glycogen to glucose
in animals

Polysaccharides : Starch structure

Polysaccharides : Glycogen
structure

Polysaccharides: Cellulose
structure

Polysaccharides: Chitin
Structure

PROTEIN

PROTEINS

Composed of chains
of amino acids
20 amino acids exist
Amino acids contain
Central Carbon
Amine group
Carboxyl group
R group

The 20 Amino Acids

All differ with respect to their R group

PEPTIDE BONDS OCCUR

BETWEEN AMINO ACIDS

The COOH group

of 1 amino acid
binds to the NH2
group of another
amino acid
Forms a peptide
bond

FUNCTIONS OF PROTEINS

Enzyme catalysts specific for 1 reaction

Defense antibody proteins, other proteins
Transport- Hgb, Mgb, transferrins, etc
Support keratin, fibrin, collagen
Motion actin/myosin, cytoskeletal fibers
Regulation- some hormones, regulatory
proteins on DNA, cell receptors
Storage Ca and Fe attached to storage
proteins

THERE ARE FOUR LEVELS

OF PROTEIN STRUCTURE

Primary structure:
the linear arrangment of
amino acids in a protein and
the location of covalent
linkages
such as disulfide bonds
between amino acids.

 Secondary

structure:areas of folding
or coiling within a protein;
examples include alpha
helices and pleated sheets,
which are stabilized by
hydrogen bonding.

Tertiary structure

the final three-dimensional structure of a protein, which results from

a large number of non-covalent interactions
between amino acids.

Quaternary structure

non-covalent interactions that bind multiple

polypeptides into a single, larger protein.
Hemoglobin has quaternary structure due to
association of two alpha globin and two beta

LIPIDS

LIPIDS

Central core of glycerol

Bound to up to 3 fatty acid chains
They exhibit a high number of C-H bonds
therefore much energy and non-polar
When placed in water, lipids spontaneously
cluster together
They help organize the interior content of
cells phospholipids

GLYCEROL AND FATTY ACID

CHAINS

SATURATED AND UNSATURATED FATS

The difference resides in the number of

Hs attached to Cs in the fatty acid
chains; the amount of saturation on the
Cs

SATURATED VS
UNSATURATED FATS AND
DIET

Saturated fats raise LDL-cholesterol levels in the

blood (animal fats, dairy, coconut oil, cocoa butter)
Polyunsaturated fats leave LDL-cholesterol
unchanged; but lower HDL-cholesterol (safflower
and corn oil)
Monounsaturated fats leave LDL and HDL levels
unchanged (olive oil, canola, peanut oil, avocados)
One variety of polyunsaturated fat (Omega-3 fatty
acids) guards against blood clot formation and
reduce fat levels in the blood (certain fish, walnuts,
almonds, and tofu)

PHOSPHOLIPIDS AND
CELL MEMBRANES

P-lipids make up the majority of cell

membranes including:
The plasma membrane
Nuclear envelope
Endoplasmic reticulum (ER)
Golgi apparatus
Membrane-bound vesicles

CELL ENVIRONMENT
ORGANIZES
P-LIPID BILAYER TO
PROPER ORIENTATION

Hydrophilic (polar)
heads of P-lipid
oriented to the
exterior; hydrophobic
(non-polar) tails
oriented to the
interior

NUCLEIC ACIDS: DNA AND RNA

DNA =
deoxyribonucleic acid
DNA is a double
polymer (chain)
Each chain is made of
nucleotides
The 2 chains bond
together to form a
helix

DNA NUCLEOTIDES
Each nucleotide in
DNA contains:
5-C sugar
(deoxyribose)
Phosphate
Nitrogen base
-adenine (A)
-guanine (G)
-cytosine (C)
-thymine (T)

One polymer of nucleotides on

one backbone of nucleic acid

MEMBERS
RATTIYAKORN INTHASRI
M.6/1 NO.39
NATTANAN SITTAPIROM
M.6/1 NO.41