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Biological Molecules

The Building Blocks of Life


• Atoms of carbon, hydrogen, oxygen, and a
few other elements bond together covalently
to make the biological molecules.
• Monomers (small molecules, such as glucose)
bond together to form polymers (large chain
molecules, such as complex carbohydrates).
• The four classes of biological molecules are
carbohydrates, lipids, proteins, and nucleic
acids.
Synthesizing & Digesting:
Two basic reactions:
1) Dehydration
synthesis
– Dehydration – water
lost
– Synthesis - build
• = removing a water
molecule to build a
polymer!!
Synthesizing & Digesting:

2) Hydrolysis
– Hydro – water
– Lysis – break apart
• = Using water to break apart polymers!
• DIGESTION!!!!!!!!
BIOMOLECULES
1. Any organic molecule that is produced, used or
functioning in a biological organism
2. Molecules containing Carbon, Hydrogen,
Nitrogen, and Oxygen.
2. They make up living organisms Examples:
Methane (CH4) Glucose (C6H12O6) are all organic
molecules
3. Carbon is the central atom and will bond
covalently because of the 4 valence electrons
(outermost shell)
4. CHONP
Carbohydrates
Carbohydrates
► CH20

► i.e. starch, cellulose

► roles/functions: basic components of protoplasmic


structures of nucleic acids and nucleotides; serves as
immediate source of chemical energy (glucose) in
living systems

► divided into three major classes


monosaccharides
► mono – “single” or “simple;
saccharide – “sugar”
► most important as building block for
more complex carbohydrates
► glucose
► galactose
► fructose
disaccharides
► di – “double”; saccharides – “sugar”
► double sugars formed by the linking of
two simple sugars
► important as building blocks and cellular
fuels
► glucose + glucose maltose
► glucose + galactose lactose
► glucose + fructose sucrose
Polysaccharides
► poly – many; saccharides – sugars
► long chains of glucose linked together (polymer)
► empirical formula: (C6H10O5)n
► Functions/roles: structural (cellulose and chitin);
storage (glycogen and starch); cell identification
tags (polysaccharides on cell membranes); and can
be synthesized and degraded by ezymes
Cellulose

► major component of plant


cell walls
cell wall

Cellulose
chitin
► major component of some
arthropods exoskeleton
Mannan
► consists mainly of mannose; makes up the cell walls of
various microorganisms
starch
► stored sugar in plant cells
 stored sugar in animal cells
Lipids: Hydrophobic molecules
► 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”
Lipids
► fatty acids
► neutral fats (triglycerides) – energy
storage, insulation, cushioning,
protection for various parts
► phospholipids – cell membrane
structure
► cholesterol – constituent of cell
membrane; synthesized by most cells
► hormones - steroids
What is a Fatty Acid?
long hydrocarbon chain capped by a carboxyl
group (COOH).

important sources of fuel because, when metabolized,


they yield large quantities of ATP

Types of fatty acids:

 Saturated fatty acids

Unsaturated fatty acids


saturated fatty acids
saturated with hydrogen (since double bonds
reduce the number of hydrogen on each carbon)
i.e.  cheese, butter, lard,  coconut oil,
chocolate,  pizza,dairy desserts, bacon and 
sausage and fatty meats.

Unsaturated fatty acids


with at least one double bond within the fatty
acid chain
i.e. avocado, nuts, and vegetable oils
Phospholipids and cell membranes

► P-lipids(amphipathic) 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
Fake fat?

What do you see in this molecular structure


that suggests why Olestra is not digested?
Why might it cause the symptoms
described on the label?
Proteins
are very important biological
molecules that play crucial
roles in virtually all
biological processes
BIOLOGICAL FUNCTIONS OF PROTEINS

1. Catalytic function:
Nearly all chemical reactions in biological systems are catalyzed
by specific enzymes.

2. Transport and storage:


For example;
 Hemoglobin transports oxygen in erythrocytes
 Myoglobin carries & stores oxygen in muscle.
 Albumin transports free fatty acids in blood.
 Transferrin transports iron in blood.

3. Coordinated motion:Actin and myosin are contractile proteins in


muscle.
BIOLOGICAL FUNCTIONS OF PROTEINS

4. Structural and Mechanical support:


For Example; collagen, a fibrous protein in skin and bone.

5. Defense function:
For Example Clotting factors prevent loss of blood.
Immunoglobulins protects against infections.

6. Generation and transmission of nerve impulses:


For example, rhodopsin is the photoreceptor protein in retinal
rod cells.

7. Control of growth and differentiation:


For Example
 growth factor proteins.
 hormones such as insulin and thyroid-stimulating
hormone.
Enzymes
Activation Energy
 Chemical reactions in cells cannot
start without help
 Activation energy gets a reaction
started
Characteristics of Enzymes
Energy In, Energy Out
 Exergonic reactions:
 produce more energy than they use
 positive flow of energy from the system to
the surroundings. 
 Endergonic reactions:
 use more energy than they produce
 requires energy to be absorbed in order
for it to take place.
KEY CONCEPT
 Most chemical reactions that sustain
life cannot occur unless the right
enzymes are present
How Enzymes Work
 Substrates:
 reactants in enzymatic reactions
 Active site:
 a location on an enzyme that fits a
particular substrate
Active site
Amino acids

How Enzyme (E) Substrates (S)

Enzymes Enzyme-substrate
complex (E-S)

Work
H2O

Free enzyme (E)

Peptide bond

Internal rearrangements
leading to catalysis

Dipeptide product (P)


There are four levels of protein
structure
► Primary = sequence of
aa’s
► Secondary = forms
pleated sheet, helix, or
coil
► Tertiary = entire length
of aa’s folded into a
shape
► Quaternary = several
aa sequences linked
together
Biological classification
1- Non essential amino acids: These are
Glycine, Alanine, Serine, Tyrosine,
Cysteine, Arginine, Asparagine, Aspartic,
Glutamic acid , Glutamine and Proline.
2- Essential amino acids:
They include Valine, Leucine, Isoleucine,
Threonine, Methionine,, Lysine, Histidine,
Phenylalanine and Tryptophan.
Metabolic classification
 Glucogenic amino acids: These amino acids could
give intermediates which finally can give glucose.
 Purely ketogenic amino acids: They include
Leucine & Lysine. They give ketone (organic
compound containing a carbonyl group =C=O) bodies
after its degradation in the body, but no glucose.
 Mixed amino acids: These are amino acids that can
give both ketone bodies and glucose intermediates.
These are Phenylalanine, Tyrosine, Tryptophan,
Isoleucine and Lysine.
* The rest of amino acids are all purely
glucogenic (an amino acid that can be converted
into glucose)
RNA
DNA RNA
Permanent form of genetic Impermanent form of G.I.;
information; stable rapidly destroyed in cell
molecule

Repository of genetic RNA can be assembled


information passed from into a chain using existing
generation to generation DNA chain as template

Acts as template for RNA Several types each with


synthesis different role in protein
synthesis
DNA RNA
Composed of a base, deoxyribose, Composed of a base, ribose, and a
and a phosphate phosphate

Consists of two strands of Consists of a linear arrangement of


nucleotides running in opposite nucleotides
directions

Purines (adenine and guanine) Purines (adenine and guanine)

Pyrimidines (thymine and cytosine) Pyrimidines (uracil and cytosine)


REVIEW

Monomers Polymers Examples

Complex Starch,
Simple sugars
Carbohydrates Cellulose, etc.

Hemoglobin,
Amino acids Proteins
Keratin, etc.

Fatty acids & Fats, waxes,


Lipids
glycerol oils, steroids.

Nucleotide Nucleic Acids DNA, RNA

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