The Importance of Domain Knowledge

• Most of you are coming to this class with a strong

background in quantitative fields

• There is incredible demand in academia and industry Math

for persons with strong quantitative skills who can
apply these skills to biology and biomedicine Statistics

• In order to properly and efficiently apply quantitative Programming

skills to the study of biology and biomedicine, you
must have some domain knowledge Engineering

• Domain knowledge will keep you from wasting your

time doing irrelevant/uninteresting analyses and it will
enable you to spend your time doing analyses that are
interesting will lead to meaningful insights into how
biology works and how we can do a better job treating
patients
An Exciting Time to Be Combining Quantitative Skills and Biology

All patients receive an untargeted

cytotoxic drug(s). Usually based
on tissue of origin of cancer

Cancer Patients
 An Exciting Time to Embark on a Biomedical Research Career

All patients receive an untargeted

cytotoxic drug(s). Usually based
on tissue of origin of cancer

Targeted Therapy A
Biostatistics
Cancer Patients Bioinformatics Targeted Therapy B
Domain Knowledge

Tumor Targeted Therapy C

Biopsy
Sequencing
 Improvements in Lung Cancer Overall Survival Times
• In stage IV lung cancer, patients
treated with traditional chemotherapy
survive ~9-12 months

• New targeted therapies have greatly

improved survival outcomes for
some patients

• Still much work to be done as these

results are only for patients whose
lung cancer has a mutation in the
EGFR gene

• We want these survival curves to be

flat lines starting at 100% and
remaining there
Soria et al. New England Journal of Medicine. Osimertinib in
Untreated EGFR-Mutated Advanced Non–Small-Cell Lung Cancer
A Whirlwind Tour of Biochemistry
Stephen Guest, Ph.D.
August 12, 2019

2019

Digital Art/Getty Images

What are we talking about when we talk about Biochemistry?

All of the chemical reactions that

take place inside of living cells
that make life possible

Biochemistry seeks to understand

all of these processes at their
most basic level

Starting with the most

fundamental units that make up
living cells – the elements

Human cells growing in culture

Nature Methods 11, 731–733 (2014) 
 Elements Are the Fundamental Building Blocks of the Cell
• What is an element?

• Elements are defined as

substances that cannot easily be
broken down or converted to other
substances

• Elements are the fundamental

building blocks of a living cell

O
pretty
easy
O really
hard

H H H
H
 Building Blocks of Life

• Lego analogy: Each element can

be thought of as being like an
individual Lego piece

• Each piece is very hard to break

apart

• However, it is easy to combine

them together
 Four Elements Dominate in Living Organisms
• 98 different, naturally occurring
elements have been discoved on
Earth

• Fortunately, the overwhelming

majority of matter inside of living
cells is composed of only four
elements: Hydrogen, Carbon,
Oxygen, and Nitrogen aka the Big
Four
 The Big Four

http://www.rsc.org/education/teachers/resources/jesei/minerals/students.htm

This composition is very different from the composition of the non-living world
 Elements are Extremely Small

One hydrogen atom is ~.2nm in diameter so 5x10^6 hydrogen atoms end-to-end = 1mm

Because they are so small, there is no way to directly visualize elements

 A Schematic View of One Atom of Hydrogen
Understanding H, C, N, & O is the key to understanding all of Biochemistry

Let’s take a close look at one atom of Hydrogen

Every element is defined by the number of protons

- and electrons that it is composed of

Hydrogen is the simplest element

Electron +
One atom of hydrogen has a nucleus with a single
proton that is orbited by a single electron
Proton

Hydrogen Protons have positive charge while electrons have

atomic number = 1 negative charge
 A Closer Look at the Big Four
• Understanding H, C, N, & O is the key to understanding all of Biochemistry

Hydrogen
atomic number = 1
 A Closer Look at the Big Four
• One atom of the element Carbon has a nucleus with 6 protons orbited by 6 electrons

Hydrogen
atomic number = 1

Carbon
Atomic number = 6
 A Closer Look at the Big Four
• One atom of the element Nitrogen has a nucleus with 7 protons orbited by 7 electrons

Hydrogen
atomic number = 1

Carbon
Atomic number = 6
 A Closer Look at the Big Four
• One atom of the element Nitrogen has a nucleus with 7 protons orbited by 7 electrons

Hydrogen
atomic number = 1

Carbon Nitrogen
Atomic number = 6 Atomic number = 7
 A Closer Look at the Big Four
• One atom of the element Oxygen has a nucleus with 8 protons orbited by 8 electrons

Hydrogen
atomic number = 1

Carbon Nitrogen Oxygen

Atomic number = 6 Atomic number = 7 Atomic number = 8
 Elements Interact with Each Other to Form Molecules
• Cells are not just bags full of elements
• For the most part, cells don’t contain a lot of elements floating around as individual atoms
• Most of a living cell is composed of elements that have been linked together to form molecules
 Elements Interact with Each Other to Form Molecules
• Molecules are groups of atoms that have been bonded together
• When H, C, N, and O are bonded together in different ways they can form all of the
important molecules that make up a living cell

DNA

Proteins

Lipids
 Electrons Are Organized Into Orbital Shells
• Electrons play the key role in determining how elements bond with each other to form molecules
• To understand how elements bond to each other, we must understand the concept of an orbital shell
• Orbital shells are defined regions around the nucleus where electrons can exist
• Electrons don’t get to orbit the nucleus anyhere they want
• Each electron of an element must exist in something called an orbital shell
• There are only 2 orbital shells that we need to know about today: orbital shell #1 and orbital shell #2

Orbital Shell #1
Orbital shells in this schematic
are represented as rings around
the nucleus

The first orbital shell is the

closest to the nucleus and can
hold 2 electrons

The 2nd orbital shell is further

and can hold 8 electrons
Orbital Shell #2
 Some Key Points

Orbital shells can be empty, full, or partially full

Electrons in partially full orbital shells are highly reactive i.e.

they are anxious to form bonds

Electrons in full orbital shells are highly stable/not reactive i.e.

they’re not really looking to form a bond
 Electrons Are Organized Into Orbital Shells
• In hydrogen, the first orbital shell has one electron
• The first orbital shell can hold two electrons
• This means that hydrogen’s electron is in a partially full orbital shell = highly
reactive

Orbital Shell #1
Hydrogen

Orbital Shell #2
 Electrons Are Organized Into Orbital Shells
• If we compare this to an element like Helium (atomic number = 2) it has two
electrons
• Because the first orbital shell holds two electrons, the first orbital shell is full
• This means that helium’s electrons are in a full orbital shell = highly unreactive

Orbital Shell #1
Hydrogen Helium

Helium is one of the inert gases

Orbital Shell #2
 Looking at Orbital Shells for the Big Four
Hydrogen Carbon
• Orbital shells are
always filled from the
inside out

• Carbon has 6 electrons

so we place the first 2
into the 1st orbital shell
and the remaining 4
Nitrogen Oxygen into the 2nd orbital shell

• Notice that all 4 of these

elements have partially
filled orbital shells
Another Way of Looking at Orbital Shells

Molecular Biology of the Cell. 4th edition.

Figure 2-4 Filled and unfilled electron shells in some
common elements
 Schematics Are Cumbersome
• All good scientists are inherently lazy
• Therefore, when drawing elements we typically don’t draw out all of the protons
and electrons of the element
• Instead, a shorthand called the Lewis Dot Structure is used
• In a Lewis Dot Structure we write the symbol of the element and use dots to
represent the electrons
• The catch is that we ONLY draw the electrons in the outermost orbital shell

= H = C
Hydrogen
Carbon has 4
Hydrogen has
1 electron in
Carbon electrons in
outermost shell outermost shell
Lewis Dot Structures for Nitrogen and Oxygen

= N = O

Nitrogen Oxygen

Electrons in the outer orbital

shell have a special name.
They are called the valence
electrons of an atom
 Sharing of Electrons Forms a Covalent Bond
We mentioned that a partially full orbital shell is highly reactive. Why is that?
Elements with partially full orbital shells will try to share electrons with other elements in such such a
way as to achieve a full outer orbital shell

• Looking at an example, hydrogen

needs one electron to fill its’
H O H outermost shell

• Oxygen needs two electrons to fill its’

outermost shell

• Hydrogen and Oxygen can share

electrons to achieve full outer shells
 Sharing of Electrons Forms a Covalent Bond
We mentioned that a partially full orbital shell is highly reactive. Why is that?
Elements with partially full orbital shells will try share electrons with other elements in such such a
way as to achieve a full outer orbital shell

• Looking at an example, hydrogen

needs one electron to fill its’
H O H outermost shell

• Oxygen needs two electrons to fill its’

outermost shell

• Hydrogen and Oxygen can share

electrons to achieve full outer shells
H OH
• When atoms share electrons like this
they form what is called a covalent
bond (sharing valence electrons)
 Sharing of Electrons Forms a Covalent Bond
We mentioned that a partially full orbital shell is highly reactive. Why is that?
Elements with partially full orbital shells will try share electrons with other elements in such such a
way as to achieve a full outer orbital shell

• Looking at an example, hydrogen

needs one electron to fill its’
H O H outermost shell

• Oxygen needs two electrons to fill its’

outermost shell

• Hydrogen and Oxygen can share

electrons to achieve full outer shells
H OH
• When atoms share electrons like this
they form what is called a covalent
bond (sharing valence electrons)

H O H = H O H Our first molecule

More Examples of Covalent Bonds Between the Big Four
How can carbon and hydrogen How can nitrogen and hydrogen
share electrons to obtain complete share electrons to obtain complete
outer orbital shells? outer orbital shells?

C H N H

H H
HCH H C H HNH H N H
H H H H
Methane Ammonia

Carbon tends to form 4 covalent bonds Nitrogen tends to form 3 covalent bonds
 Atoms Can Form Double Covalent Bonds

O C
Sometimes two atoms will
share more than one electron
to form something known as a
double covalent bond
O C O

C Carbon Dioxide
O O
 Carbon is the Most Versatile of the Big Four
The ability to form 4 covalent bonds makes Carbon the most versatile
C element of the big four

• Carbon readily forms four covalent bonds

• This allows carbon to form a wide range of different

and useful shapes:

-It readily forms long, linear chains with itself

-It readily forms branched tree structures that
can go off in any direction
-It readily forms ring structures

• There’s no obvious limit to the size of these

Molecular Biology of the Cell. Alberts structures.

This versatility is likely the reason that we are carbon-based life forms
 Covalent Bonds Can Be Polar or Non-Polar
•
•
In a covalent bond, two elements are sharing electrons H OH
This sharing of electrons is not always equal
• Some elements hold onto electrons more tightly than others
• They are said to be more electronegative
• Within the big 4, N and O hold onto electrons much more tightly than H and C

Electronegativity of the big 4

H=C<N=O
 Covalent Bonds Can be Polar
• When a bond is formed between two elements with similar electronegativity, the electrons are shared
equally and this is called a non-polar covalent bond

Electronegativity of the big 4

H=C<N=O

H
H C H
H
Covalent bonds between H and C
are non-polar

Methane is a non-polar molecule

 Covalent Bonds Can be Polar
• When a bond is formed between two elements with different electronegativity, the more
electronegative element will hold the shared electrons closer. Result is a polar covalent bond.

Electronegativity of the big 4

H=C<N=O

Oxygen is winning
H (+) (-) (+)
the tug of war

H O H
H C H
H Covalent bonds between H and O
are polar

Covalent bonds between H and C Water is a polar molecule

are non-polar
H gets a slight (+) charge and O
Methane is a non-polar molecule gets a slight (-) charge
 Water Water Everywhere Water

• We know that human cells contain

mostly H, C, N and O

• We know that these elements

combine to form molecules

• What is the most abundant molecule

in the cell?

• By far, the answer is water. ~70% of

all molecules in the cell are water
molecules
 What’s So Special About Water?
• Both covalent bonds in water are polar covalent bonds
• This gives the two hydrogen atoms a slight positive charge
• And the oxygen atom gets a slight negative charge
• This is important because the positive charge on a H atom of one water molecule can
interact with the negative charge on an O atom of a different molecule of water
• This interaction is called a hydrogen bond (much weaker than covalent bonds)
• Hydrogen bonds are what give water many of its’ special properties
• Without hydrogen bonds between water molecules, life on earth would not exist
• Hydrogen bonds are weak in comparison to covalent bonds ~1/100
• Hydrogen bonds in water are continually formed and broken i.e. rearranged
 Hydrogen Bonds Give Water Important Properties
Despite the relative weakness of individual hydrogen bonds, they combine to have significant
consequences

• Without hydrogen bond interactions,

the boiling temperature for water
would be ~ negative 100 degrees C.

• So water would be a gas at

physiological conditions and life as we
know it could not exist.

• Hydrogen bonds also give water its’

relatively high surface tension

• Gerridae (aka water walkers) walking

on water
Hydrogen Bonds Don’t Just Form Between Water Molecules
Electronegativity of the big 4
H=C<N=O
Hydrogen bonds can also form (+)
between water and any molecule (+) (-) (+) H
(-)
that has a negatively charged O or N H O H ||||||||||||||||||
N H
(+)

(+)

Hydrogen Bond
H
Ammonia

(+)
(+) (-) (+)
H H
H O H ||||||||||||||||||
O (+)C H
(-)

Hydrogen Bond
H
Methanol
 Hydrogen Bonds Don’t Even Need to Involve Water
• Whenever a molecule contains a Hydrogen atom that is involved in a polar covalent
bond there’s potential for hydrogen bonds to form

• All it takes is for that positively charged H(+) to run into a negatively charged N(-) or O(-)
 There Is More to A Cell than Just Water
• After water, proteins are the 2nd most abundant molecules in a living cell

• Estimated that every cell contains between 1 and 10 billion protein molecules

• This is roughly equivalent to the number of people on planet earth

~7.6 Billion People (2018)

• Proteins are molecules that are responsible for
most of the action inside of cells and
throughout our bodies

• Proteins allow cells to generate energy

• Proteins mediate cell division, cell movement

and how cells communicate with each other

• Proteins mediate immune responses, muscle

contraction and on and on…
 What Are Proteins?
• Proteins are large molecules that are
made up from small molecules called General structure of an Amino Acid
amino acids
a-Carbon Carboxyl Group
• Amino acids are molecules that all
contain an amino group
Amino Group
• They also contain a carboxyl group

• These are linked to each other through

a central carbon atom (alpha carbon)

• There are 20 different amino acids

commonly found in human proteins

• They differ by their R groups

 Amino Acid R-Groups aka Side Chains
The really interesting part of an amino acid is the R group aka side chain

• The side chain is what makes each Glycine

amino acid unique

• Each side chain has its’ own special

H
properties

• Side chains provide incredible chemical

diversity to proteins

• They also determine the many different

shapes that proteins can take

• No need to memorize all the side chains

 Some General Principles of Side Chains

• Some amino acid side chains have Isoleucine

only non-polar covalent bonds

• Isoleucine is one example

• Because they lack polar covalent

bonds, these side chains do not H C CH3
interact well with water
CH2
• They are considered hydrophobic
(water-hating) CH3

Electronegativity of the big 4

Seven ther amino acids with hydrophobic
side chains: HAlanine,
= C < N Leucine,
=O Methionine,
Phenylalanine, Valine, Proline, Glycine 
 Some General Principles of Side Chains

• Some amino acid side chains Serine

contain polar covalent bonds

• Serine is one example

• Because they have polar covalent

bonds, these side chains interact CH2
well with water
O
• They are considered hydrophilic H
H
(water-loving) Hydrogen Bond O
H
Electronegativity of the big 4
Some other amino acids with hydrophilic side
H = C < Lysine,
chains: Threonine, N = O and Glutamate
 Some Side Chains Are Considered Special Cases
• The side chain for glycine is
simply H
Glycine
• This side chain is the least
bulky of all side chains

• This makes glycine special

because it gives a protein
lots of conformational H
flexibility

• Can be used when a protein

needs to make a ‘tight turn’
for example
 Some Side Chains Are Considered Special Cases

• The side chain for proline

actually reaches back and Proline
forms a covalent bond with
the amino group nitrogen

• This makes proline special

because the bond between
the a-carbon and the
amino nitrogen can’t rotate CH2
CH2
• Prolines can therefore give CH2
a region of a protein
rigidity
 Some Side Chains Are Considered Special Cases
• The side chain for cysteine contains
a sulfur atom Cysteine

• If there are two cysteines in the same

protein they can react to form a bond
known as a disulfide bond

• This helps a protein form specific 3-D CH2

shapes
SH
S
• Disulfide bonds can also form across
2 different proteins to link two S
different proteins together
CH2
 How Do We Use Amino Acids to Make a Protein?
• Proteins are made by combining amino acids together into long chains
• Amino acids are combined together through a covalent bond
• The covalent bond is formed by connecting the carboxyl group of one amino acid
to the amino group of another amino acid
• This process occurs with the help of an enzyme
• The reaction is known as a condensation reaction (water producing)

The bond that forms between the amino acids is a covalent bond called a peptide bond
 Repeating the Process
• Repeating this process can string amino acids into long, stable chains
• These chains are polypeptides (many peptide bonds)
• More commonly though, they are referred to as proteins
• Theoretically no limit on the length of a protein

+ Tripeptide …..Polypeptide

dipeptide Single amino acid

 Incredible Possibilities

Because there are 20 different amino acids, there are

400 hundred possible different dipeptides

Dipeptide

Tripeptide = 8000 different possibilities

Quadruplepeptide = 1.6x10^5 different possibilities

Pentapeptide = 3.2x10^6 different possibilities

• Average length of a protein in the cell is ~300 amino acids

 Beads on a String

• A protein therefore is a series of

amino acids that have been
bonded together to form a chain
that can be thought of as beads
on a string

© 2010  Nature Education All rights reserved.

 Proteins Have Two Chemically Distinct Ends
Whenever a protein is formed, one end will have an amino group, this is the amino or N-
terminus while the other end of a protein will have a carboxyl group, this is the carboxy
or C-terminus.
Because of the way they are formed, amino acids have a repeating
pattern in their backbone: Nitrogen-Carbon-Carbon-Nitrogen-Carbon-Carbon…
One of the carbon-nitrogen bonds has some double bond character
that prevents it from rotating

No Rotation
The Other Carbon-Nitrogen and the Carbon-Carbon Bonds Can
Freely Rotate
Due to This Flexibility Proteins Can Adopt Many Different 3-D
Conformations
Rotate Bonds Rotate Bonds
 To Function Properly Proteins Must Fold Into Specific Shapes
• A linear sequence of amino acids linked together to form a protein isn’t functional until it
folds into a very specific shape

Unfolded/No Structure Folded

Highly Structured

• When proteins don’t fold properly it often leads to disease

• Alzheimer’s, Parkinson’s, and ALS(Lou Gherig) can all be caused by improper
folding of proteins in the cell
 How Do Proteins Fold?
Proteins have different levels of structure called primary, secondary and tertiary

The Primary structure is simply the linear sequence of amino acids in the protein
The Secondary structure of a protein is the 3-dimensional shape that local
segments of a protein take

These local segments typically form

one of two basic structures: a-helix
or b-sheet

Notice how hydrogen bonds play a role in

forming and stabilizing these structures
Finally, there’s Tertiary structure which is the overall global shape that a
protein folds into
Two examples:

• Rhodopsin is a protein that senses light • Porins form pores in cell membranes
• It is comprised almost completely of a- that allow for transport across
helices • Porins are proteins that are comprised
almost completely of b-sheets

Most proteins contain a mix of both a-helices and b-sheets

Hydrophobic and Hydrophilic Side Chains Play a Key Role In Folding
Regions of a protein with Hydrophilic side chains will tend to be on the outside of the final tertiary structure

Regions of a protein with Hydrophobic side chains will tend to be on the inside of the final tertiary structure

Hydrophilic Hydrophobic
side chains side chains
In some proteins disulfide bonds play an important role in folding

Folded protein

Unfolded protein
 Sugar Rush
• What else do we find besides
water and proteins inside a cell?

• ~8% of the mass of a cell is made

of sugars (carbohydrates)

• Sugars such as glucose serve as

a primary energy source for our
cells
(CH2O)6 = C6H12O6 = Glucose
• Individual sugar molecules
(CH2O)5 = C5H10O5 = Ribose
(monosaccharides) all have the
same general formula (CH2O)n. (CH2O)4 = C4H8O4 = Erythrose
Hence the term carbo-hydrate
 The Basic Structure of Monosaccharides
• There are two major classes of sugars: Monosaccharides and Polysaccharides
• Monosaccharides e.g. glucose, all have the same basic structure

At one end there is a carbon atom

that is part of an aldehyde group

All of the other carbon atoms in the

monosaccharide have hydrogen atoms
and hydroxyl groups attached

Monosaccharides inside the cell are almost never found in the linear, open chain, form
shown above
In the cell, monosaccharides form cyclic structures
The oxygen in one of the hydroxyl groups reacts with the carbon in the
aldehyde group to form a ring
 Polysaccharides Are Polymers of Monosaccharides
• The other major class of sugars found in the cell are Polysaccharides
• Polysaccharides can be formed by linking monosaccharides together in a chain
• Sucrose, common table sugar, is an example of a polysaccharide
• Sucrose is formed by connecting a molecule of Glucose with a molecule of
Fructose

Forming a polysaccharide is
another example of a
condensation reaction

This forms a glycosidic bond

Lactose is another common

1 slice ~ 50grams of disaccharide. It is formed by
succrose combining glucose with
galactose
 Polysaccharides
Very Large polymers can be made by combining many monosaccharide subunits

Monosaccharide subunits can be linked

in a linear chain or in branch structures

Glycogen is a polysaccharide made up

of glucose subunits

Glycogen is a highly branched

structure used by muscle cells and
cells of the liver for long-term glucose
storage
Molecules That Store Information
 The Discovery of Nucleic Acids
In 1869 Friedrich Miescher discovered and isolated a substance from inside the
nuclei of cells that he called nuclein

He showed nuclein was composed of Hydrogen, Carbon, Nitrogen, Oxygen and

Phosphorus

He showed nuclein to have acidic properties and hence was called nucleic acid
 Another Polymer: Nucleic Acids are Polymers of Nucleotides
• Years later it was found that nucleic acid is a polymer
• Just like proteins are polymers of amino acids and and polysaccharides are polymers of
monosaccharides
• Nucleic acids are polymers that are made up from molecules called nucleotides

• Nucleotides are molecules that

contain a 5 carbon sugar (ribose)

• A phosphate group is linked to

the C5 carbon atom

• A base is linked to the C1 carbon Ribose

atom
The Identity of the Bases In Nucleotides
• There are two types of bases that can be linked to
the sugar molecule in a nucleotide:

• The Purine bases are Adenine and Guanine

• They have a double ring structure

• The Pyrimidine bases are Thymine and Cytosine

They have a single ring structure

• Note that there are many polar covalent bonds in

these molecules

Electronegativity of the big 4

H=C<N=O
• There are two types of
nucleic acids found in living
cells: RNA (Ribo Nucleic
Acid) and DNA (Deoxy Ribo
Nucleic Acid)

• The sugars of RNA and

DNA differ by only one
hydroxy (-OH) group at the
C2 carbon atom.
Nucleotide Polymers Are Formed by Condensation Reactions Between Nucleotides
A condensation reaction links the sugar of one nucleotide to the phosphate group of another
nucleotide
Repeating The Process Generates a Nucleic Acid Molecule
• A DNA molecule can be built up
by repeatedly forming bonds
between nucleotides in this
fashion.

• Notice that this molecule has a

sugar phosphate ‘backbone’

• The backbone has directionality

• The end with an exposed

phosphate group is called the 5’
end

• The other end has an exposed

hydroxyl group and is called
the 3’ end
Theoretically no limit to the length of a Nucleic Acid molecule

Each strand of human chromosome 1 contains 249 million nucleotides

Amazingly, two long molecules of DNA can interact to form a double-
stranded structure

To form this structure Thymine bases

interact with Adenine bases on the
opposing strand

And Cytosine bases interact with

Guanine bases on the opposing strand

These Interactions are mediated by H-

bonds

The interacting DNA molecules must be

anti-parallel to each other
 The DNA Double Helix
Two interacting molecules of DNA come together to form a double
helical structure
 Last But Not Least, Lipids
Lipids are the molecules in a cell that serve as biological membranes
• Lipids separate cells from
their surrounding environment

• The boundary that separates

the cell from the outside
environment is a lipid
membrane

• Lipids also allow for the

existence of specialized
compartments inside of the
cell

Lipids aren’t just membranes can also be used for energy storage and in cell signaling/communication
 What Exactly Are Lipids?
• Generally speaking, lipids are hydrocarbon molecules meaning they are made up from
combining Hydrogen and Carbon together
• Lipid molecules typically contain either long hydrocarbon chains or linked hydrocarbon rings.

Saturated lipids contain hydrocarbon chains with all single bonds

Unsaturated lipids contain hydrocarbon chains with Carbon/Carbon double bonds
 Phospholipids Are a Special Class of Lipids
Most of the lipids found in biological membranes are from a special class of lipids called phospholipids

Phospholipids typically contain two

hydrocarbon chains known as tails

The hydrocarbon tail contains mostly non-

polar bonds and is therefore very
hydrophobic

Phospholipids also have a ‘head’ group that

contains phosphate

The phosphate containing head group

always contains polar bonds that make the
head group very hydrophilic
 Phospholipids Form Ordered Structures In Aqueous Environments

Phospholipids are amphipathic meaning
they have both a polar hydrophilic end
and a non-polar hydrophobic end
Polar Head Group
(Hydrophilic)
When placed in water the hydrophobic ends will
seek to avoid water molecules
This results in self-organization of phospholipids
into structures like micelles, liposomes, and lipid
bilayers

Non-Polar Tail
(Hydrophobic)