MACROMOLECULES

UNIT 4
 Vocab
● Macromolecule: A very large molecule
composed of thousands of covalently
bonded atoms
● Monomer: a molecule that can be bonded
to other identical molecules to form a
polymer
● Polymer: a substance or material
consisting of very large molecules, or
macromolecules, composed of many
repeating subunits
● Organic molecule: a complex molecule
that is primarily made of carbon atoms
bonded with other elements and/or other
carbon atoms
Carbon’s diversity
● 4 unpaired valence electrons = many
opportunities to branch out
● This configuration allows carbon
skeletons to be formed
● Hydrocarbons are molecules of C and
H held together by nonpolar covalent
bonds
Carbon
skeletons
● They are the central
components to a molecule ● Double bond location: Placement of double
● 4 ways that skeletons vary: bonds can change the shape and function
○ Length: number of atoms of a molecule
in backbone ● Presence of rings: Skeletons may form rings
with single or double bonds
○ Branching: branches off
the skeleton change the
structure, but not
molecular formula
 Functional
Groups
● component/part of the organic molecule that is
MOST commonly involved in chemical reactions
● The number and arrangement of function groups
gives each molecule unique chemical and
physical properties
Hydroxyl Group Carbonyl Group Carboxyl Group
(OH) (C=O) (COOH)
● Reactive ● Reactive ● Reactive
● Polar/Hydrophilic ● Polar/Hydrophilic ● Polar/Hydrophilic
● Hallmark of ● Location on molecule ● Can act as an acid (donate
carbohydrates changes classification: H+ ions)
○ Within: ketone ● Ionized form in a cell has
○ End: aldehyde charge -1
Amino Group Sulfhydryl Phosphate
(NH2) Group (SH) Group (PO4)
● Reactive ● Reactive ● Reactive
● Polar/Hydrophilic ● Slightly polar/nonpolar ● Polar/Hydrophilic
● Can act as a base (accepts ● React with one another to ● Charged
H+ ions) form disulfide bridges ○ -1 within molecule
● Ionized form in a cell has ● Provide structure and ○ -2 at end of
charge +1 support to tertiary molecule
proteins
 Methyl
●
Group
Not reactive
● nonpolar / hydrophobic
● Acts as a molecular tag for
identification
○ Number and location of them
gives molecule identity
● Affects gene expression
○ Whatever it is attached to does
not present itself (gene is
turned off and protein is not
made)
What type of functional groups can be
identified?

Propionic acid
 Forming and breaking down organic
molecules

Dehydration synthesis Hydrolysis

● Synthesizes/creates a ● Adds a water molecule to
polymer break apart a polymer
● Removes a molecule of H2O
in the process

Both reactions can be sped up by an enzyme

 4 Major Macromolecules

Carbohydrates Lipids

Proteins Nucleotides
Carbohydrates
● Monosaccharides (monomer)
form polysaccharides (polymers)
● Simple sugars that 1:2:1 ratio of
C:H:O
● Glucose: extremely important
monosaccharide that is a
food/energy source for cells
○ Immediate energy source (used
in cellular respiration)
○ Formula is C6H12O6
● Disaccharides can be formed
from two monosaccharides
through dehydration synthesis
 Lipids
● Not true polymers
○ Not every lipid is made up of the
same units , and none have
similar monomers
● Lipids are all nonpolar and
hydrophobic
○ Due to hydrocarbons
● Made up of fatty acids and
glycerol most of the time
○ They are linked by Ester linkage
 Proteins
● Amino acids are the monomer
for proteins
● Amino acids are made up of:
○ A central carbon
○ An amino group (NH2)
○ A carboxyl group (COOH)
○ An R group
● There are 20 amino acids
● Peptide bonds form between
amino acids, making proteins
polypeptides
○ Bond is formed between COOH
and NH2 groups of 2 different
acids
Proteins (cont.)
● Amino acids differ based on their
R group:
○ Nonpolar side chains make the
acid nonpolar and hydrophobic
○ Polar side chains make the
amino acid hydrophilic
■ The bonds in the R group
are polar covalent bonds
■ Can form hydrogen bonds
○ Electrically charged side chains
make the acid hydrophilic
■ Acidic R-Group = negative
charge
■ Basic R-Group = positive
charge
 Nucleic Acids
● Made up of nucleotides
● Nucleotides are made of:
○ A pentose sugar adenine
■ Deoxyribose or ribose
○ Phosphate group
○ Nitrogenous base
■ Pyrimidines (1 ring)
● Thymine (DNA)/ Uracil
(RNA)
● Cytosine
■ Purine (2 rings)
● Adenine
● Guanine
GCAT
Nucleic Acids
● The pentose sugar and phosphate group of
different nucleotides are connected using a
phosphodiester bond
○ The sugar of one nucleotide to the
phosphate group of the one below it
○ This bond location causes a repeating
pattern to occur
○ Forms the sugar-phosphate backbone
that lines the outside of a
polynucleotide, so the nitrogenous
bases point inwards
■ Polynucleotides : nucleotides
linked together by
phosphodiester bond
Identify the
molecule

Phenylalanine
MACROMOLECULES
: Structure and
Function
 Carbohydrates
Serve as :
● Fuel, structural support, and building
materials for other molecules
● Polysaccharides : polymers of sugar
made up of 100s - 1000s of
monosaccharides
○ Uses glycosidic linkages
○ Long-term energy storag
○ Structural roles
○ Architecture and function are
determined by its sugar
monomers and the position of
glycosidic linkages
 4 Types of Polysaccharides

Starch

● Composed of Glycogen
alpha-glucose
monomers ● Composed of
● Amylose: unbranched alpha-glucose
● Amylopectin: slightly monomers
branched ● Highly branched, with
● Provides stockpile of many side chains
energy for plants ● Found in liver and
muscle cells
● Long term storage of
energy for animals
 4 Types of Polysaccharides

Cellulose
● Composed of Chitin
beta-glucose monomers
● Unbranched molecules:
no side chains ● Composed of
● Found in cell walls of beta-glucose monomers
plants ● Found in exoskeletons
● Microfibril : group of of insects and cell walls
of fungi
cellulose molecules that
are held together by
hydrogen bonds
 Lipids Glycerol

● Not true polymers

● Lipids serve as an energy reserve,
regulate hormones, transmit nerve
impulses, cushion vital organs, and Fatty acid
transport fat-soluble nutrients
● Triglycerides:
○ One glycerol molecule and three
fatty acids bound by ester linkages
○ Glycerol: a 3-carbon molecule with
an OH group at each end
○ Fatty acid: hydrocarbon chain with
a carboxyl group at the end
■ hydrophobic
Triglyceride
Saturated Fats Unsaturated Fats
● Completely saturated ● Has one or more double
hydrocarbon chain bonds in the hydrocarbon
● All single bonds between chain
carbon atoms ● Double bonds cause a bend in
● Very straight and can be tightly the chain
packed ● Cannot pack tightly
● Solid at room temperature ● Liquid at room temperature
Proteins
● Proteins send signals, assist reactions,
provide structure, and transport
chemicals
● Polypeptide: polymer of amino acids that
is joined together by peptide bonds
● Proteins are not functional when they are
just polypeptide chains
○ Specific activities of proteins result
from their 3D shape
■ A polypeptide chain must be
folded, twisted, maneuvered,
etc. to become functional
through 3 (4?) steps
Primary Protein Structure
(nonfunctional)

● Simple, linear polypeptide chain

● Amino acids linked by peptide bonds
● Order of the amino acids is determined
by DNA (→RNA)
● Primary protein structure determines the
shape at higher levels
● 1D
Secondary Protein Structure
(nonfunctional)

● Occurs due to the formation of hydrogen bonds

in specific locations
○ Due to the partial positive of the amino
group and the partial negative carboxyl
group
○ Hydrogen bonds are connecting peptides
● Alpha-Helix
● Beta-Pleated Sheet
● 2D shapes
○ Different shapes depend on where the
hydrogen bonds occur
■ Deals with what amino acids are
present in the polypeptide structure
Tertiary Protein Structure
(functional)

● Occurs due to R-Group interactions (turns into a

3D shape)
● Hydrogen Bonds : between polar R-groups
● Ionic Bonds : between electrically charged
R-groups
● Nonpolar Interactions & Vans der Waals
Interactions : between nonpolar R-Groups
● Disulfide Bridges : between cysteine amino
acids
○ Cysteine contains a sulfhydryl (SH)
functional group
○ SH react with one another to form cross
links that make disulfide bridges
Quaternary Protein Structure
(functional)

● Not found in ALL proteins

● Occurs due to reactions between 2+
polypeptide chains that are at tertiary
structure
○ Must interact with each other to
function
● Ex: hemoglobin : the 4 MUST come
together in order for hemoglobin to
function
○ 2 alpha polypeptide chains
● 2 beta polypeptide chains
● Chemical and physical environments can denature
proteins
○ Denaturation: process that causes weak bonds
of a protein to break and unravel
○ Proteins lose their function and structure
■ Ex: through heat, altered pH
level, etc.
○ Some proteins may undergo renaturation
Nucleic Acids

● Composed of nucleotides
○ Phosphodiester bonds hold the
sugar-phosphate backbone
together
● Polynucleotides have directionality (5’ →
3’)
○ 5’ end has a free phosphate group
(PO4)
■ Comes off the 5th carbon
○ 3’ end has a free hydroxyl group
(OH)
■ Comes off the 3rd carbon
DNA (deoxyribonucleic
acid)
● Stores and expresses hereditary/genetic
information
● Directs cell function
● Directs RNA synthesis
● Contains bases (A→T / G→C)
● Pentose sugar : deoxyribose
● Made of 2 anti-parallel strands that run
opposite of each other
○ Wraps around in a helix
● Opposite strands are held together by
their complementary base pairs using
hydrogen bonds
RNA (ribonucleic acid)

● Directs protein synthesis

● Contains bases (A→U / G→C)
● Pentose sugar : ribose
● Made up 1 strand of polynucleotides
○ Wraps around itself, so the bases
pair with the strand itself
○ Can take on many unique
shapes/structures
● Nitrogenous bases held together by
hydrogen bonds
ATP (adenosine triphosphate)

● Composed of adenosine, ribose, and 3 phosphate groups

○ The negative charges amongst the phosphate
groups makes ATP very unstable and easy to break
○ Water can easily break apart this unstable ATP to
release energy
● Stores energy for the potential to react with water and
release energy for the cell to use to do work
● To release energy, ATP undergoes hydrolysis
○ Water is added to an ATP molecule and the
terminal phosphate group breaks off, which
releases energy
○ Turns into ADP (adenosine diphosphate), an
inorganic phosphate, and energy
■ Energy is used to now work within the cell
■ Exergonic: releases energy
○ Building ATP from ADP + P + Energy is endergonic
because it takes in energy to accomplish