Intro to

Biochemistry
Deschampions AP Biology
 Topic 1.2
Elements of Life
★ Learning Objective ENE-1.A: “Describe the composition of
macromolecules required by living organisms.”
 Biochemistry Intro
question
Question: What are atoms and why are
they important to living organisms?
Think about the question
Pair- Share your answer with your shoulder
partner
Share- I will call on someone to share their
answer.
 ★ Smallest stable unit
of matter that has
the characteristics
of its specific
element
★ Structure: Nucleus
with electron
orbitals.
○ Protons are
positively charged
Atoms ○ Neutrons are
neutral and have
Or…. What is the smallest unit of matter that biochemists care about for 800, Alex?
 ○ Electrons are
negatively
charged
○ Each orbital has a
different amount
of energy
associated with it.
■ Closer to the
nucleus = lower
energy level
Atoms orbital
■ Farther away=
Or…. What is the smallest unit of matter that biochemists care about for 800, Alex?
 Valence
★ Valence electrons
Electron ○ Found in the
outermost orbital
★ Used for making
different types of
bonds!
★ Most elements want 8
electrons in their
valence shell because
Atoms this makes them the
most stable.
Or…. What is the smallest unit of matter that biochemists care about for 800, Alex?
Have a positive Have more
Cations
Protons than
(+ )Charge Electrons
★Atoms are usually
neutral
○# electrons = # of
Ions
protons
★Non-neutral
atoms are called
ions. Two Types.
Have more Have a
Anions
Electrons negative (-)
than Protons charge
 Elements of Life
Main Elements of life:
Carbon, Hydrogen, Oxygen, Nitrogen (CHON)

★ All the others are trace

elements
○ Found in small
(trace) amounts in
the body
○ BUT they are critical
to maintaining
homeostasis.
 photosynthesis
○ Incorporated into
carbohydrates
○ Main source of biomass
in ecosystems
★ Organisms utilize carbon to
produce every
biomolecule
(carbohydrates, proteins,
The Importance nucleic acids, lipids)
★ When organisms die,
of carbon decomposers recycle the
Or…. Why Carbon is the basis of organic life forms
carbon back into the
environment.
★ Organisms is carbon-
 ★ Inorganic nitrogen is
fixed from the atmosphere
by bacteria and other
decomposers and
absorbed by plants to enter
the food web.
★ Organisms utilize nitrogen
to produce proteins and
nucleic acids.
The Importance ★ Nitrogen is recycled into the
environment by
of Nitrogen decomposers.
★ Organisms in nitrogen
Or…. why nitrogen is important FOR THE GAINS
depleted areas will die
because they cannot make
 ★ Phosphorus is used to build
nucleic acids and certain
types of lipids
(phospholipids) .
★ Organisms in phosphorus
depleted areas will die
because they cannot make
The Importance nucleic acids or
phospholipids (the major
of Phosphorus component of cell
Or…. why life as we know it would not exist without phosphorus membranes).
You Practice: Think, Pair,
Share

Think to yourself: How are

the chemicals secreted by
the fish being used by the
plant in this aquarium?
Pair: Share your answers
with your shoulder partner.
Share: Deschamps will call
on students to share their
The figure shows a model of the exchange of matter between the organisms that live
together in an aquarium. The model includes matter exchange between plants, fish,
and bacteria. The bacteria are represented as rod-shaped organisms living in the gravel
at the bottom of the aquarium.

Which of the following statements best describes how molecules released by the fish become
nutrients for the plants?

A. The carbon dioxide molecules released by the fish are converted by the bacteria to
oxygen atoms, which are used by the plants to make water molecules.
B. The oxygen molecules released by the fish are converted by the bacteria to
ammonia molecules, which are used by the plants to make lipids and fatty acids.
C. The nitrites released by the fish are converted by the bacteria to carbon dioxide
molecules, which are used by the plants to make carbohydrates.
D. The ammonia molecules released by the fish are converted by the bacteria to
 ★ Electronegativity is the
measurement of how
strongly atoms attract
bonding electrons to
themselves.
○ i.e. It’s the measurement
of how much they will
pull electrons toward
themselves.
Electronegativi ★ Determined by how many
electrons are in the
ty valence shell.
★ The closer to eight
Or…. probably the single most important chemistry concept
to understand if you want to be able to understand anything electrons they have, the
in this unit, biochemistry, organic chemistry (basically any
chemistry) more electronegative the
element is.
Electronegative Elements you need to know

Fluori Oxyge Nitrog

ne More n en
Most electronegative Least
electronegative than nitrogen electronegative
element!!! of the three.
Less
Not common in electronegative Still a very
Biology, but I than fluorine, electronegative
expect you to more element though
know it anyway. electronegative
than nitrogen.
 Electropositivity
A measurement of the ability of elements to donate
electrons and form positive ions.

★ These elements usually

have 1 or 2 electrons in
their valence shells.
★ They are NOT very
electronegative.
Electrons
and
Bonding
 Ionic bonds are
weaker than
Occur when two Covalent covalent bonds
atoms share and will dissociate
electrons Bonds in water, so we
don’t see them
alot in biology.
Covalent
Bonds vs.
Energy is Ionic Bonds
stored in Transfer of
valence
covalent bonds Ionic Bonds electrons from a
and is released metal to a non-
when the bond metal
 ★ Polar molecules occur
when there is
unequal sharing of
electrons across a
covalent bond.
★ Happens when a very
electronegative
element is bonded to
Polarity a very small OR very
electropositive
AKA a direct consequence of electronegativity that is
super important to how life as we know it operates. element.
 OVERALL NEUTRAL
CHARGE
★ BUT they have partial
negative and partial
positive charges on the
poles.
★ Electronegative element
will be partially negative
because it is pulling

Polarity
electrons toward itself.
★ Electropositive element
will be partially positive
AKA a direct consequence of electronegativity that is
super important to how life as we know it operates. because it has less
electron density near
 Hydrogen bonds
Weak attraction between a hydrogen bonded to an
oxygen (O), Nitrogen (N) or Fluorine (F) and
another O, N or F atom.
★ Why only O, N and F?
○ They are very
electronegative.
○ Hydrogens bonded to them
have a partial positive
charge.
○ O,N and F in other areas
have a partial negative
 Bonds and Molecular Shape
★ How atoms are bonded
together determines their
overall shape.
★ The structure, shape and
chemical properties of a
molecule determines the
function of that molecule.
○ This is super important and will
show up over and over again
 Laws of Conservation

★ Energy is ALWAYS conserved in a reaction.

○ Energy that appears “lost” was probably given off as heat.
★ The amount and types of atoms are conserved in a
reaction.
○ If you start with two oxygens and four hydrogens, you must end with
the same (unless more are added in)
★ The amount of bonds in a chemical reaction are conserved.
○ If you start with four bonds, you end with four bonds.
 Any
Questions?
★ Contact Deschamps
Properties of
Water
Deschampions AP Biology
 Topic 1.1
Structure of Water and Hydrogen Bonding
★ Learning Objective SYI 1.A: “Explain how
the properties of water that result from its
polarity and hydrogen bonding affect its
biological function.”
Properties of Water Intro
question
Question: What are some roles that
water plays
Think aboutorganisms
in keeping the question
alive?
Pair- Share your answer with your shoulder
partner
Share- Deschamps will call on someone to
share their answer.
 ★ Water is an important
component in many
chemical reactions
that help organisms
maintain
homeostasis.
★ Water allows for the
transport of
How does Water materials in different
organisms.
support Life? ○ Blood in animals
○ Sap in plants
 ★ These partial charges on the
poles attract to opposite
charges on other molecules
nearby
★ Water’s polarity allows it
to hydrogen bond with
○ Other water molecules
○ Other polar or charged
molecules
★ These chemical properties
allow water to
Chemical ○ Exhibit cohesion and
properties of adhesion
○ Have surface tension
Water ○ Resist temperature
Or…. why is water uniquely suited to support life? changes
Water molecules This is why
are attracted to Cohesion water will
and can hydrogen adhere to other
bond with other molecules and
water molecules surfaces.
Water exhibits
Surface tension
Cohesion
capillary action
in water is directly
because it is
causedvs.
by the fact
capable of both
that water is
Adhesion
cohesion
cohesive.
and
This is why adhesion. Water molecules
water sticks are attracted to
together as a Adhesion and can hydrogen
fluid and forms bond with other
droplets on polar or charged
 Surface Tension
Cohesion of water molecules at the surface of a
body of water
★ Water molecules on the surface
are surrounded by air on one
side.
★ Because they hydrogen bond
with fewer neighbors, the h-
bonds are stronger.
★ This allows water to have a
defined surface that resists
being ruptured by light objects
 Capillary Action
★ Water adheres to the side
of tubes that are lined
with polar/charged
molecules and “crawls”
up the tube. The water
molecules do not
separate because of
cohesion. This is called
capillary action.
★ Plants take advantage of
capillary action to pull
water from the roots
and into their vascular
 collectively strong.
★ Liquid water has lots of
hydrogen bonds that are
constantly breaking and
reforming.
★ It takes A LOT of energy to
break all of the hydrogen
bonds and cause water to
evaporate into steam.
★ This is what causes water
to resist temperature
Water Resists change so well.
○ AKA High Specific Heat
Temperature Capacity
Changes ★ This is useful for living
Or…. how does water help organisms maintain a constant internal temperature organisms that need to
 ★ Water is an excellent solvent
because it is polar.
○ Solvent = substance
that dissolves other
chemicals.
★ Very good at pulling ionic
compounds (like salt) apart
into ions.
○ Ions are “electrolytes”
○ Required for life
★ Can also create a water shell
around polar molecules that
Solvency of cannot ionize because they
are held together by
Water covalent bonds.
Or…. why do so many chemicals dissolve in water? ○ Like Sugar, which we use
 Topic 1.1 Main
Concepts
★ Water’s polarity is directly responsible for its ability to
hydrogen bond
○ Can H-Bond with other water molecules and other
charged/polar molecules that are nearby.
★ Water’s polarity and hydrogen bonding are directly
responsible for its ability to support living systems
through:
○ Cohesion/Adhesion
■ Which allow for capillary action and surface tension
○ Solvency (ability to dissolve polar compounds)
○ Water resisting temperature changes.
 Any
Questions?
★ Contact Deschamps
Biomolecular
Metabolism
Deschampions AP Biology
 Topic 1.3
Introduction to Biological Macromolecules
★ Learning Objective SYI 1.B: “Describe the
properties of the monomers and the type of
bonds that connect the monomers in
biological macromolecules.”
 Biomolecule Intro
Question
Question: What are biomolecules, and why do
you think they are important for maintaining
Think- Silently think
homeostasis of an
in living answer for the
organisms?
question
Pair- Share your answer with your shoulder
partner
Share- Selected students share answer with
the class.
 ★ Organic, carbon
based
macromolecules.
○ Organic = can be
used and converted
by living things
★ All living organisms
need biomolecules!
★ Four main types
What is a ○ Carbohydrates
Biomolecule? ○ Lipids
○ Proteins
 for bonding.
★ Therefore carbon always
forms 4 covalent bonds.
○ Hydrogen only forms 1
bond
○ Oxygen usually forms 2
bonds
○ Nitrogen usually forms 3
bonds
★ Carbon based molecules can
form a variety of different
structures because of its
Why Carbon ability to form four bonds.
★ More available structures
Though? = more available
Or…. why are all known life forms carbon based? functions =
 Biomolecule Terminology
Mono Polym
Dimer
mer er

individual two many

subunit monomers monomers
(building covalently covalently
block) of a bonded bonded
biomolecule together together
 Biomolecule Metabolism
The combination of chemical reactions that
synthesize and hydrolyze biomolecules for energy
storage and release in an organism.
Catabolic are endergonic,
reactions break meaning they
down biological Catabolism require a net
polymers into investment of free
monomers to help energy into the
Exergonic reactions bonds between the
generate ATP. Free
release energy
free energyis
monomers
Catabolism
energy
that that by
is used is
actually available
endergonic
vs.soto they
reactions
for a cell use
Anabolism
can
for
called
occur. This is
metabolic
Catabolic processes reaction Anabolic reactions
coupling.
reactions are build up
exergonic, Anabolism monomers into
meaning there biological
is a net release polymers for
 Dehydration Synthesis
Process by which monomers are covalently bonded
together into polymers
★ Dehydration synthesis is an
anabolic process that
synthesizes polymers for
energy storage and/or
structure
★ Requires the assistance of
enzymes
★ Dehydration = removal of
water, Synthesis = to
make (a bond)
○ Dehydration synthesis is
 Hydrolysis
Process by which polymers are broken down into
monomers.
★ Hydrolysis is a catabolic
process that breaks down
polymers to release energy
★ Requires the assistance of
enzymes and the breakdown
of water to occur.
★ Hydro = water,
Lysis = to break (a bond)
○ Hydrolysis uses water to
break the bond between
 Topic 1.3 Main
Concepts
★ Free energy is energy that is available to do work in a cell.
★ Exergonic and endergonic reactions are coupled together
○ Exergonic reactions release free energy that is captured and used to
make endergonic reactions able to occur.
★ Dehydration synthesis is an anabolic chemical reaction that forms
covalent bonds between monomers to build polymers of
biomolecules.
○ Water is formed as a byproduct of the reaction.
★ Hydrolysis is a catabolic chemical reaction that breaks the covalent
bonds between monomers to break polymers into monomers.
○ Water is used as a reactant in the reaction.
★ Both dehydration synthesis and hydrolysis require the assistance of
 Any
Questions?
★ Contact Deschamps
Biomolecules

Deschampions AP Biology
 Topic 1.4 and 1.6
Properties of Biological Macromolecules and Nucleic Acids
★ Learning Objective SYI 1.B: “Describe the
properties of the monomers and the type of bonds that
connect the monomers in biological macromolecules.”
★ Learning Objective IST 1.A:Describe the structural
similarities and differences between DNA and RNA.
 Biomolecules Intro
question
Question: What are some types of
biomolecules you know about, and what
Think
are about the question
they used for?
Pair- Share your answer with your shoulder
partner
Share- Deschamps will call on someone to
share their answer.
 ★ Carbohydrates are commonly
referred to as sugars.
★ Monomers =
monosaccharides
○ Simple sugars like glucose
★ Polymers = polysaccharides
○ Complex carbohydrates like
starches, cellulose, etc.
★ Structure
○ Hexamer Rings

Carbohydra ★ Main Functions

○ Short term energy source
○ Energy storage

tes ○ Structure
■ Cellulose in plants
■ Chitin in insects/ crabs
 ★ Elemental Composition
○ Carbon, Hydrogen,
Oxygen
○ 1C: 2H: 1O ratio
○ E.g. C6H12O6
★ Glucose is a monosaccharide
that is broken down during
aerobic cellular respiration
to help make ATP energy.
★ Carbohydrates are also
Carbohydra found in small amounts on
the cell membrane and help

tes cell types recognize each

other.
 carbohydrates stability,
Energy storing allowing for the
carbohydrates Energy formation of tough
structures that allow for
have a branched Energy
Storing structural support. We
see this in plant cell
structure.
Storing
Carbohydrate walls and chitin shells in
crabs.
vs. s

Structural Cellulose
More branches means Structural
more monomers can Carbohydrat carbohydrates
be broken off at once,
allowing for cellular
Structural
es have a linear
respiration to happen Carbohydrate structure and
faster to make more are able to
 ★ Monomers are fatty acids
★ Polymers are lipids
★ Main Functions
○ Long term energy
storage
○ Insulation and protection
of organs
★ Structure
○ Long hydrocarbon
chains

Lipids ★ Elemental Composition

○ Carbon, Hydrogen,
Oxygen
○ 1C: 2H: very little
 ★ Phospholipids are a
special type of lipid that
make up the main part of
the cell membrane.

★ Lipids are hydrophobic,

Lipids meaning they avoid water.

★ Saturated and unsaturated
fats are lipids that show up
in many foods.
 The double bonds in
Saturated fats unsaturated fats
do not have Saturated prevents them from
stacking, so they are
double bonds in
their molecular Fats liquid at room
temperature. They are
structure. Saturated
“Bad Fats” less likely to clog your
arteries and veins.
Fats
Vs
Unsaturate
Saturated fats are
linear, which means d Fats Unsaturated
fats do have
they can stack and
form solids at room
Unsaturated double bonds in
temperature. This can Fats their molecular
lead to lipid build up
structure.
 ★ Proteins are commonly
found in meats and
muscles.
★ Monomers = amino
acids
★ Polymers =
polypeptides
★ Structure
○ Very complex with four
levels
○ More on this later
★ Elemental Composition

Proteins ○ Carbon, Hydrogen,

Oxygen, Nitrogen
and Sulfur
 ★ Main Functions
○ Wounds and tissue
repair
○ Catalyzing chemical
reactions
○ Cell Signaling
★ Enzymes are
specialized proteins
that speed up
(catalyze) chemical
reactions in cells to help
maintain homeostasis

Proteins ★ Some proteins are

embedded in the cell
membrane and help with
 ★ Nucleic acids are commonly
referred to as genetic
material.
★ Monomers = nucleotides
○ 3 Parts of a
Nucleotide
■ Sugar
■ Phosphate
■ Nitrogenous Base
○ 3 parts linked by
covalent bonds

Nucleic ★ Polymers = nucleic acids

★ Elemental Composition
○ Carbon, Hydrogen,
Acids Oxygen, Nitrogen and
Phosphorous
 ★ Main Functions
○ Storage of genetic
material
★ There are two types of
nucleic acids: DNA and
RNA
★ DNA and RNA have
Nucleic directionality
○ 5’ end and 3’ end

Acids
 Deoxyribonucleic Acid (DNA)
vs. Ribonucleic Acid★ Single
★ DNA Structure
(RNA) Stranded
○ Eukaryotes: Linear, double ★ 3 Types of RNA
stranded double helix ○ Messenger RNA
○ Prokaryotes: Circular, double
stranded double helix. (mRNA)
★ Stores the genetic ○ Transfer RNA
code (tRNA)
★ 4 nucleotides ○ Ribosomal RNA
○ Adenine
DNA (rRNA)
○ Thymine
★ Used for protein
○ Cytosine
○ Guanine synthesis
★ Nucleotides have a ★ 4 nucleotides
deoxyribose sugar ○ Adenine
★ More stable than RNA ○ Uracil
★ Location ○ Cytosine
○ Eukaryotes: Nucleus
○ Prokaryotes: Floating in the ○ Guanine
cytoplasm of the cell ★ Nucleotides have a
ribose sugar in them
Identify the Macromolecule….
Carb, Protein, Lipid, NA? Subcategory?
 You Practice (Think, Pair,
Share)
Think to yourself: Which
part(s) of the nucleotide
could you examine to figure
out if this nucleic acid is DNA
or RNA.

Pair: Share your answers

with your shoulder partner.

Share: Deschamps will call

on students to share their
Figure 1. Nucleic acid fragment
answers
 Figure 1 (to the left) represents a
nucleic acid fragment that is made
up of four nucleotides linked
together in a chain.

Which of the following

characteristics of Figure 1 best
shows that the fragment is RNA
and not DNA?

A. The 5’ to 3’ orientation of the

nucleotide chain
B. The identity of each nitrogenous
base
C. The charges on the phosphate
groups
Figure 1. Nucleic acid fragment D. The type of bond linking the
nucleotides together.
Biomolecules, Food, and Calories
The energy we get from breaking down biomolecules is
called “Calories”.
★ These are the same as calories in
food.
★ Lipids, Carbohydrates and Proteins
are all broken down by the body
for energy.
○ Lipids have the most energy
■ 9 calories in 1 gram of fat
○ Carbohydrates and proteins
have the same amount of
energy
■ 4 calories in 1 gram of
sugar/ protein
 Comparing and Contrasting Biomolecule functions

Instructions: Put an X in each box that correctly represents a function of the corresponding
biomolecule.
Can be
Helps Part of the
Energy Codes for broken
catalyze Cell
Storage Traits down for
reactions Membrane
energy

Carbohydra
te X X X
Lipid X X X
Protein X X X
Nucleic
Acid X
 Any
Questions?
★ Contact Deschamps
Structure and Function of
Proteins
Deschampions AP Biology
 Topic 1.5
Structure and Function of Biological Macromolecules
★ Learning Objective SYI 1.C: “Explain how a change
in the subunits of a polymer may lead to changes in
structure or function of the macromolecule.”
 Proteins Intro question
Question: What do you think would
happen to an organism with a mutated
DNA Polymerase protein?
Think about
(DNA polymerase the question
helps synthesize new
Pair- Share your answer
DNA)with your shoulder
partner
Share- Deschamps will call on someone to
share their answer.
 ★ 4 levels of protein
structure
○ Primary
○ Secondary
○ Tertiary
○ Quaternary*
★ Each level builds on the
others.
★ Each level is held
Protein together by different
bonds and interactions
Structure formed between
amino acids.
 ○ N terminus is located
at the first amino
acid in the chain
■ Amine group is free
○ C terminus is located
on the last amino
acid in the chain
■ Carboxyl group is
free
Protein ★ All proteins have

Structure primary, secondary, and

tertiary structure.
 Hydrogen
★ Present because carbon
★ Amine
NH2 or NH3
★ Theremust form
are 20 4 bondsamino
common Carboxyl
★ Group acids in organisms. ★ Group
COOH or COO-
Amine =
★ Each amino acid has the same ★ AKA Carboxylic
contains
“peptide backbone” structure Acid
nitrogen
made of the ★ Capable of
★ Capable of ○ Amine Group
hydrogen hydrogen
○ Carboxyl Group
bonding bonding
○ A hydrogen
★ Amine groups ★ The only difference between each ★ Carboxyl found
found in the “R” of the amino acids is the in the “R” side
side chain will structure and chemical chain will usually
R Side Chain be negatively
usually be properties
★ Structureof varies
the R Side Chain
positively charged
between each of the 20
charged common amino acids
★ More on these later :)
 R Group Properties
The chemical properties and bonding abilities of the amino
acid (AA) side chains are determined by the elemental
Hydrophobi composition. Acidic
Look for: Hydrophilic (Hydrophilic)
c Look For:
★ Long Look for:
hydrocarbon ★ Oxygen or ★ Carboxyl Groups
chains (C and H nitrogen in the ★ Negative
only) side chain charges
★ Big hexamer ★ No charges Basic
rings (Hydrophilic)
Look For:
★ Amine Groups
★ Positive
Charges
Instructions: Look at the side chain in each box and determine if it is
hydrophobic, hydrophilic, acidic, or basic. Please also determine if the
side chain is capable of hydrogen bonding.

Property: ______________________ Property: ______________________

Capable of H-Bonding: Capable of H-Bonding:
____________ ____________

-
Property: ______________________ Property: ______________________
Capable of H-Bonding: Capable of H-Bonding:
____________ ____________
Primary protein Structure
★ Primary protein structure
is the sequence of
amino acids formed via
protein synthesis.
★ The amino acid
sequence is what
determines how the
protein folds at all
levels.
★ Changing the amino
acid sequence will
Formation of the Primary protein Structure
★ Primary structure is formed
when two amino acids are
covalently bonded
together via dehydration
synthesis.
○ Peptide bond =
covalent bond formed
between two amino
acids.
★ Requires the help of
enzymatic RNA in ribosomes.
★ Peptide bond forms
 Secondary Structure

★ Secondary structure occurs Can hydrogen bond to other amino

acids in the protein
as the protein begins to fold
★ Protein is not active yet
★ Two secondary structures:
○ Alpha helices
○ Beta pleated sheets
★ Held together by hydrogen
bonding between the
carboxyl and amine groups
on the peptide backbone
★ No R-groups involved.
(2o) Structure Close-up

Examples of backbone
hydrogen bonding are
outlined in red.

Peptide backbone outlined in black.

 Tertiary Structure

★Tertiary structure occurs as

the protein finishes folding
★Proteins are usually
functional at this point.
★Tertiary structure is
controlled by interactions
between the R side chains
on the amino acids.
★Hydrophobic collapse is
the major driving force
behind formation of the
tertiary structure.
 Hydrophobic Collapse
Occurs as the hydrophobic amino acids collapse away from
the water and into the interior of the tertiary structure of
the protein.

UNFOLDED FOLDED

Black circles: Hydrophobic amino acids

White Circles: Hydrophilic amino acids
 between side chains
with electronegative
atoms (O and N)
★ Charge attraction
between acidic (-) and
basic (+) charges
★ H-bonds and charge
attractions are sensitive

R Group to changes in pH and

temperature and will be

interactions
broken if the protein is
outside of the normal
 ★ Disulfide bridges are
covalent bonds
between the sulfur
atoms present in the
side chains of two
cysteine amino acids.
★ Disulfide bridges are
R Group very strong and are
not sensitive to
interactions: changes in pH or
Disulfide Bridges temperature.
 ★ More disulfide
bridges = stronger
structure
★ Cysteine AA’s do not
have to be near each
other in the sequence
to form the bond.
R Group ★ Usually found in
proteins exposed to
interactions: harsh conditions
Disulfide Bridges ○ High temperature
 Quaternary Structure
★Quaternary structure occurs when
multiple proteins come together
to form a protein complex.
○These proteins are all folded at
the tertiary level.
★Not all proteins are involved in
quaternary structures.
★Held together by interactions
between the variable side
chains and hydrogen bonding
Each of the different colors above
between the peptide backbones represents a tertiary protein.
of the different proteins.
 Any Questions?
★ Contact Deschamps