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2 Biomolecules

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0% found this document useful (0 votes)
10 views64 pages

2 Biomolecules

Uploaded by

ernestmajor75
Copyright
© © All Rights Reserved
We take content rights seriously. If you suspect this is your content, claim it here.
Available Formats
Download as PDF, TXT or read online on Scribd

Monomers, polymers, and

macromolecules

Rodgers Mengwa
REFERENCES :

1. Principles of biochemistry (Lehninger), A. L., Nelson, D.


L., & Cox, M. M. (2000). Lehninger. New york: worth
publishers.
2. Biochemistry by U satyanarayana; u chakrapani. New
delhi : elsevier health sciences APAC, 2013
3. Fundamentals of biochemistry by J.L. Jain, sunjay jain,
nitin jain,s.Chand. Edition 2005.

9/19/2023 RMCM 2
Atoms to Molecules
Functional Groups

Functional groups
determine how a
molecule will
interact with other
molecules.

Why does sugar dissolve in water?


Fig. 3.1

Functional groups:
Carbon is the central element
• All biomolecules contain a Carbon chain or ring
• Carbon has 4 outer shell electrons (valence = 4)
• Therefore it’s 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
CH4 =
Carbon linkages
Propane
• Single chains
• Rings = C3H8

The 4 types of biomolecules often


consist of large carbon chains
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

Amino acid

OH, NH2, PO4 are called ‘functional groups’!


Isomers
• Isomers have the same molecular formulas but different structures
• Structural isomer = difference in the C skeleton structure
• Stereoisomer = are isomeric molecule that have the same molecular
formular and sequence of bonded atoms, but differ in three-dimensional
orientation of their atoms in space.
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
Examples: amino acids (L
form)
sugars (D form)
Monomers and polymers
• Monomers are made into polymers via dehydration reactions
• Polymers are broken down into monomers via hydrolysis
reactions
Isomers
1. Mention and illustrate all possible
structural isomers from C6H14.
2. What is the number of possible structural
isomers for bromopentane?
3. What is the number of possible structural
isomers for C3H9N?
Organic Molecules
• Any molecule containing
carbon is called an organic
molecule
!! Except CO2 !!
• Most organic molecules are
arranged like chains
– Each link is a monomer
– A chain is a polymer
– A large molecule made of a
long chain or chains is a
macro molecule
Types of Organic Molecules
• Carbohydrates
• Lipids
• Nucleic acids
• Proteins
Carbohydrates
• Molecules used for energy, made of C H O
– Monosaccharide: a simple sugar (glucose, fructose, galactose)
– Disaccharide: two monosaccharides bound together (sucrose aka
table sugar)

– Polysaccharide: 3 or more monosaccharides (starch is hundreds of


glucose molecules bonded together)
Fig. 3.5

Examples of sugar monomers*

*Remember how C’s are counted


within the ring structures (starting
from the right side and counting
clockwise)
Carbohydrates (sugars)

• Double sugars
(disaccharides)
• Two 6-C chains or
rings bonded together
Carbohydrates (sugars)
• Complex carbo’s
(polysaccharides)
– Starch
– Cellulose
– Glycogen
– Chitin

Glycogen to glucose
in animals
Fig. 3.9
Polysaccharides
Starch structure vs Glycogen structure
Fig. 3.10

Polysaccharides: Cellulose structure


Proteins
• Composed of chains
of amino acids

• 20 amino acids exist

• Amino acids contain


– Central Carbon
– Amine group
– Carboxyl group
– R group
What Are Proteins?
• Large molecules
• Made up of chains of amino acids
• Are found in every cell in the body
• Are involved in most of the body’s
functions and life processes
• The sequence of amino acids is determined
by DNA
Structure of Proteins
• Made up of chains of amino acids;
classified by number of amino acids in a
chain
– Peptides: fewer than 50 amino acids
• Dipeptides: 2 amino acids
• Tripeptides: 3 amino acids
• Polypeptides: more than 10 amino acids
– Proteins: more than 50 amino acids
• Typically 100 to 10,000 amino acids linked together
• Chains are synthesizes based on specific
bodily DNA
Peptide Bonds Link Amino Acids
• Form when the acid group (COOH) of one
amino acid joins with the amine group
(NH2) of a second amino acid
• Formed through
condensation
• Broken through
hydrolysis
Condensation and Hydrolytic
Reactions

Figure 6.3
Essential, Nonessential, and
Conditional
• Essential – must be consumed in the diet
• Nonessential – can be synthesized in the
body
• Conditionally essential – cannot be
synthesized due to illness or lack of
necessary precursors
– Premature infants lack sufficient enzymes
needed to create arginine
R-groups
determine the
properties of
individual
amino acids.
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
Denaturing
• Alteration of the protein’s shape and thus
functions through the use of
– Heat
– Acids
– Bases
– Salts
– Mechanical agitation
• Primary structure is unchanged by
denaturing
Denaturing a Protein
Heat, acidity, or both can denature proteins. Denaturing
changes the shape of a protein, which changes its
appearance and functionality. Denaturing is what happens
when we fry an egg (egg whites contain albumin protein)
or use acids to turn milk into cheese (milk solids contain
casein proteins).
The shape of a protein determines its function.

•The shape of an individual protein is determined by the


order of amino acids in the primary chain, which affects how
the amino acid chain twists and folds into the final shape of
the protein.
•DNA contains the code that instructs the cell machinery to
put amino acids together in a particular order to make a
particular protein.
•As long as the DNA contains the correct code, the protein
will function.
•Mistakes in the code (mutations) change the order of
amino acids, which changes the structure of the protein,
which prevents the protein from carrying out its function.
There are at least 7 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
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
Difference between DNA & RNA
• RNA contain the sugar ribose while DNA
contains deoxyribose (ribose that lacks one
oxygen atom)
• RNA contain uracil while DNA contains
thymine
Nucleotides link together to form nucleic acids. The
sugars bind to the phosphate groups to form the
backbone of the chain.
DNA nucleotides
• Each nucleotide in
DNA contains:
– 5-C sugar
(deoxyribose)
– Phosphate
– Nitrogen base
-adenine (A)
-guanine (G)
-cytosine (C)
-thymine (T)
Fig. 3.14

One polymer of nucleotides on one “backbone” of nucleic acid


Fig. 3.15

The DNA “double helix”


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”
Glycerol and fatty acid chains

What specific bonds form between glycerol and


each fatty acid chain?
Would you think this to be an hydrolysis or a
dehydration synthesis rxn?
Saturated and unsaturated fats

The difference resides in the number of H’s attached


to C’s in the fatty acid chains; the amount of
“saturation” on the C’s
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 (sunflower
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
Structure of single P-lipid

The 3 C’s of glycerol are bound to:


2 fatty acid chains
phosphate
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
Summary

Group work
Monomers
Simple sugars, such as
glucose, are the
monomers of complex
carbohydrates.

Label a hydrogen group


and hydroxyl group on
the glucose diagram.
What are some
properties of these
groups?
What is similar about
these four simple
sugars?
What is different?
glucose fructose sucrose

What process do you see happening here to create this


glycosidic linkage between the two sugars?

What is the scientific term for a pair of monomers linked


together?
Glycosidic linkages between many
sugar molecules create complex
carbohydrates, such as starch.

What is the scientific


term for many
monomers linked
together?
What do you see in the structure of cellulose that tells
you that it is a carbohydrate?

How is cellulose similar to starch?


Cellulose vs. Starch

We can digest starch (amylose) but not cellulose.


What difference do you see that might be the reason
behind this?
White death?
Some people claim that sugar is harmful, toxic,
or addictive. Is it?

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Label a methyl group and a hydroxyl group on one
of the fatty acids. What are some properties of
these groups?

What process
do you see
happening here
to create these
ester bonds
between the
fatty acid chains
and the glycerol
in this
triglyceride?
Lipids
• Shortening and margarine labels often brag that
their products are made with healthy,
unsaturated vegetable oils. Vegetable oils are
liquid at room temperature. So why are
shortening and margarine solid at room
temperature?
• List some examples of lipids or fatty acids – not
the foods that contain them, but specific lipids.
• How are carbohydrates and lipids different from
one another?
Phospholipids
Saturated or
unsaturated?

Label the phosphate group


on this phospholipid. What
are some properties of this
group?
Monomers

Amino Carboxylic acid


group group

Amino acids are the monomers of proteins.


On your diagram, label the amino group and the
carboxylic acid group. What are some properties of
these groups?
What process do you see happening here to create this
peptide bond between the two amino acids?

What is the scientific term for many monomers linked


together?
Monomers
Label the parts
on this
nucleotide.

Is this a
nucleotide of
DNA or RNA?
How can you
tell?
DNA is two strands of
nucleotides side-by-
side.

What is the type of


bond that forms the
cross-links holding the
two strands together?
Learning objectives
1. Know how molecules are formed
2. Know four categories of biomolecules
3. Know different types of bonds existing in
each of the four biomolecules
4. Explain and illustrate different type of
isomerisms

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