biological molecules . CARBOHYDRATES, FATS AND PROTEINS. includes how large molecules are made from smaller ones, their functions, etc. made in a very interactive way so that students can understand and clear all their concepts.

3. CARBON OXYGEN HYDROGEN

4.  Short term energy supply
› Glucose produces ATP energy
 Short term energy storage
› Glycogen is stored in the liver and muscles
 Structure
› Plant cell walls, insect exoskeletons
 Cell Membrane markers
› Cell “identity tags”

All carbs have the formula Cn(H2O)n

5. HYDROGEN + CARBON + OXYGEN =
FATS
=

6.  Long term energy storage
› Pack energy into a small space
 Insulation and Padding
› Protects organs
 Structure
› Cell membranes
 Chemical Messengers
› Steroids
 All lipids do not dissolve in water =
hydrophobic

7. CARBON + OXYGEN + HYDROGEN + NITROGEN
+ SULPHUR

8.  Starch is the nutrient storage form of
carbohydrates in plants.
 Glycogen is the nutrient storage form of
carbohydrates in animal.
 Cellulose is a rigid, structural carbohydrate
found in the cells walls of many organisms.
 Proteins are an extremely diverse group of
biological molecules composed of the small
molecules called amino acids.

9.  Proteins are created by linking together amino
acids into protein links called polypeptide chains.
There are twenty amino acids of which 12 can be
synthesized by the human body and 8 must be
ingested in the foods we eat. These 8 are referred
to as the essential amino acids.

10.  Sequences of amino acids are strung together to
produce polypeptide chains, which then fold up into
working proteins.
 Important groups of proteins include enzymes, which
hasten chemical reactions, and structural proteins,
which make up such structures as hair.
 The primary structure of a protein is its amino acid
sequence; this sequence determines a protein’s
secondary structure—the form a protein assumes
after having folded up
 The activities of proteins are determined by their
final folded shapes.
 Antibodies help to fight diseases.

12. ala
ala
gln
gln
ile
ile
. . . produces a polypeptide chain like this:
A typical protein would
consist of hundreds of
amino acids
The linkage of several
amino acids . . .

13. Figure 3.20
Primary structure
Secondary structure
Tertiary structure
(a)
(b)
(c)
(d) Quaternary structure
amino acid sequence
beta pleated sheet
alpha helix
random coil
folded polypeptide
chain
two or more
polypeptide chains
Four Levels of Structure In Proteins
The primary structure of any
protein is simply its sequence
of amino acids. This sequence
determines everything else
about the protein’s final shape.
Structural motifs, such as
the corkscrew-like alpha
helix, beta pleated sheets,
and the less organized
“random coils” are parts
of many polypeptide
chains, forming their
secondary structure.
These motifs may persist
through a set of larger-scale
turns that make up the
tertiary structure of the
molecule
Several polypeptide chains
may be linked together in a
given protein, in this case
hemoglobin, with their
configuration forming its
quaternary structure.

14.  There are about 20 different amino acids, each
with a different chemical structure and
characteristics; for instance, some are polar,
others are non-polar. The final protein structure is
dependent upon the amino acids that compose it.
Protein function is directly related to the structure
of that protein. A protein's specific shape
determines its function.
 antibodies and enzymes are proteins.

15. Defensive proteins/anti bodies
Virus
Antibodies
Bacterium
Function: Protection against disease
Example: Antibodies inactivate and help destroy
viruses and bacteria.