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Biochemistry Unit:
An emergent property is one which arises from the interaction of "lower-level" entities, none of which
show it.
• Life itself is an example of an emergent property. For instance, a single-celled bacterium is alive,
but if you separate the macromolecules that combined to create the bacterium, these units are
not alive.
• Metabolism, the totality of an organism’s chemical reactions, is an emergent property of life
that arises from interactions between molecules within the cell
Chemistry of Water
1. Polar covalent bonds within water
-Between slightly positive hydrogen atoms and slightly negative oxygen atom
2. Hydrogen bonds between water molecules
-Hydrogen bonds are electrical attractions between the hydrogen atom of one water
molecule and the oxygen atom of a nearby water molecule
-they create a structural organization of water that leads to its emergent properties
-weaker than polar covalent bonds
*One water molecule can form 4 hydrogen bonds
3. “Bent” geometry
O
H H
4. Polar molecules
-Water molecules have a partial charge
-Oxygen has a partially negative charge (δ—) and hydrogen has a partially positive
charge (δ+) because oxygen is more electronegative (which means it attracts electrons
more)
δ+ INTER-molecular
INTRA-molecular — attractions
δ —
= oxygen
attractions δ
Polar Covalent bond Hydrogen bond = hydrogen
+
-between hydrogen and
oxygen of the same atom δ+ -between hydrogen
and oxygen of
δ +
δ
different atoms

5. An attraction may exist between water molecules – depending on temperature

-At higher temperatures, molecules are farther apart
-When temperature decreases, kinetic energy and speed decrease, so entropy
decreases (which means molecules are more organized and closer together)
-As this happens, water goes from a gas to a liquid to a solid
Properties of Water
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1) Cohesion/ Adhesion
2) Specific heat
3) Heat of vaporization
4) Less dense as a solid
5) Universal solvent
6) Neutral pH
*Explain each property of water and relate to its importance in biology
Cohesion and Adhesion
 Cohesion- water molecules stick to each other
-They stick to each other due to the constant of forming and reforming of hydrogen
bonds that hold the molecules close together.
 Adhesion- water molecules stick to other things
 Capillary tubes:
-they have a tiny diameter: water molecules are smushed together in a small space 
they stick to each other better
-xylem = water conducting tissue
Importance in Biology:
 Cohesion and adhesion help transport water upward through plants (to the leaves)
-Water hits the ground and moves to the roots by diffusion
-Water moves up the roots and is pulled up through the stems to the leaves because of
their attractions to each other and the stem walls. This is called capillary action.
-This allows plants to produce glucose and oxygen in a process called photosynthesis.
 Transpiration pull is the main way water travels to the leaves though.
-This process is: As water is lost in the stem, it’s pulled up through the roots. This allows
there to be a constant flow of water.
 Cohesion and adhesion are the reason for water’s high surface tension
-benefits organisms who can walk on the surface of water
-soap breaks surface tension

Specific Heat and Heat of Vaporization

 Heat is a measure of the total amount of kinetic energy
Temperature measures the average amount of kinetic energy
-Temperature is measured using a Celsius scale
-Water boils at 100ºC and freezes at 0ºC
-A calorie (cal) is the amount of heat energy it takes to raise 1 g of water 1ºC

 Specific heat – amount of heat required to change the temperature of 1 gram of water by 1ºC
**Involves change in temperature
-It takes a lot of energy to change the temperature of water (exactly 1 cal)
Because a lot of energy must be absorbed to break hydrogen bonds, and a lot of
energy is released when forming hydrogen bonds
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-Water’s specific heat is very HIGH  water is resistant to temperature change

 Vaporization or evaporation occurs when molecules of a liquid with sufficient kinetic overcome
their attraction to other molecules and escape into the air as gas
 Heat of vaporization – amount of energy required to convert 1 gram of water to 1 gram of
water vapor
**Involves change in phase
-Takes a lot of energy to change phase (exactly 4.18 J/g/ ºC or 580 cal/g/ºC)
Because a lot of heat must be absorbed to break hydrogen bonds, allowing
water molecules to escape into the gas phase
-Water’s heat of vaporization is very HIGH  it’s very resistant to phase change
Importance in Biology:
 Specific heat moderates temperature:
-In coastal areas, water and land temperatures are more moderate and mild than inland
areas
 For aquatic organisms, water temperature is usually constant:
-they don’t have to adapt to wildly changing temperatures (like terrestrial animals do)
-they have less coping mechanisms
 Evaporative cooling helps protect terrestrial organisms from overheating and contributes to the
stability of temperatures in lakes and ponds
-As a liquid vaporizes, the surface left behind loses the kinetic energy of the escaping
molecules, cooling it down
 Water takes a long time to evaporate because of its high heat of vaporization
**Water-based organisms are resistant to evaporation
-Large bodies of water like the ocean do not evaporate
-When water finally does evaporate, it takes away heat from its surroundings;
conversely, when water condenses and it rains, it releases heat to its surroundings

Less Dense as a Solid

 As water freezes it expands  Hydrogen bonds pushed apart, creating a fixed crystalline
structure. The INTER-molecular attractions are stronger and more stable, creating more space.
 So ice floats.
Importance in Biology
 Floating ice insulates the liquid water below, preventing it from freezing and allowing life to
exist under the frozen surface.
COLD AIR
COOL AIR

Ice insulates the colder

WARM AIR
pond, allowing life
Ice melts  Colder water sinks
to exist under the
and warmer water rises
surface. colder
November -This is called SPRING
warmer OVERTURN. It re-
circulates nutrients.
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The warm water at the surface becomes
colder and the bottom warms up  Colder
water sinks and warmer water rises
March -This is called FALL OVERTURN. It
also re-circulates nutrients.
 Change in temperature = increases the average kinetic
Changewarmer energy of molecules (increases speed)
in phase ΔT
Change
October  Change in phase = disrupts hydrogen bonds
Temperature in phase ΔT
ΔT  But the structure of water never changes because
covalent bonds are very strong
Time

 Cellular Respiration:
C6H12C6 + O2  CO2 + H2O + ATP (energy)
-Fish get oxygen from underwater plants, not by breaking down water molecules.

Universal Solvent
 Water is the solvent in an aqueous solution
-A solution is a liquid homogeneous mixture of 2 or more substances
-The solvent is the dissolving agent and the solute is the substance that is dissolved
 Hydration shell: the water molecules surround and break up the solute molecules
-This happens because the positive and negative regions of water molecules are
attracted to oppositely charged ions or partially charged regions of polar molecules
-for example: NaCl dissolves in water.
-Water molecules surround the NaCl molecules the slightly negative oxygen
atoms are attracted to the positive Na atoms, while the slightly positive hydrogen
atoms are attracted to the negative Cl atoms  this pulls the NaCl molecules apart
 “Like dissolves like”
-Polar solvents dissolve polar solutes and ionic solutes
-Nonpolar solvents dissolve nonpolar solutes
-This is why oil (nonpolar) and water (polar) don’t mix
Hydrophilic = has an affinity for water due to electrical attractions and hydrogen bonding
-Polar and ionic substances are hydrophilic
-Large hydrophilic substances may not dissolve, but become suspended in an aqueous
solution forming a mixture called a colloid
Hydrophobic = does not easily mix with or dissolve in water
Importance in Biology
 Nonpolar and polar interactions help transport nutrients
-Nutrients diffuse across cell membranes

Neutral pH
 A water molecule can dissociate into a hydrogen ion, H+, and a hydroxide ion, OH–.
-Water has a neutral pH of 7 and the concentrations of [H+] to [OH–] are the same. [H+] = [OH–]
An increase in [H+] results in a decrease in [OH–] (and vice versa)
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When acids or bases dissolve in water, the H+ and OH– balance shifts.
-Acids donate H+ ions leading to excess of H+ ions and a pH below 7.0. [H+] > [OH–]
-Some bases accept H+ ions and some add OH– ions leading to excess of OH– ions and a
pH above 7.0. [H+] < [OH–]
-Because cells are mostly water, most cells have an internal pH close to 7.

Importance in Biology
 Keeps cells functioning at a neutral pH
-This is one of the reasons why most body fluids are around 7
 Buffers are chemicals that prevent pH from changing too much
-Buffers may be acid-base pairs which accept excess H+ ions or donate H+ ions when H+
concentration decreases
Carbonic acid (H2CO3) is an important buffer in living systems. It moderates pH changes
in blood plasma and the ocean.

-enzymes are very pH sensitive, so the pH must be constant

Chapter 4
Organic chemistry is the study of carbon compounds.
 Compounds on can either be inorganic or organic. If it’s organic, it contains carbon and involves
living things and often H and O as well.
 The Miller Urey Experiment
-It was designed to test the Halding hypothesis (Halding’s hypothesis: the atmosphere
contains hydrogen, not oxygen)
-They found that you can take inorganic molecules and get organic molecules (contain
H, C, O, and N)
-This is an example of molecular evolution, science as a process, and science,
technology, and science
Chemistry of Carbon
 Has 4 valence electrons (=outermost energy level)
Methane:
H 4 single nonpolar
. Its electron configuration:
This electron
covalent bonds,
.C. . 1s22s22p2
configuration allows
carbon to form 4
LIKE: H C H symmetrical,
tetrahedral shape
bonds with other
atoms. This is called H It exists as a gas
because it’s not
carbon’s tetravelence.
attracted to itself.
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Carbon atoms can form diverse molecules by bonding to four other atoms.
 Carbon has 4 valence electrons, so it can form at most 4 covalent bonds. This tetravalence
allows the formation of large, complex, diverse molecules.
 Carbon can form single, double, or triple covalent bonds.
-4 single bonds around carbon creates a tetrahedral shape.
-A double bond between carbons leads to a flat molecule.
 Carbon can bond with other elements and other carbons  forms short or long chains,
branches, and rings
 Carbon skeletons can vary in:
1) Length
2) Branching
3) Placement of double bonds
4) Location of atoms of other elements

Molecular Diversity Arising from Carbon Skeleton Variation

Hydrocarbons
 Hydrocarbons consist of only carbon and hydrogen
 The nonpolar C – H bonds in hydrocarbon chains result in their hydrophobic properties
-Many cells have hydrocarbon regions, like the hydrophobic fatty acid tails
 Hydrocarbons can undergo reactions that release a large amount of energy.
-In fats, hydrocarbons help cells store fat molecules as a reserve. The fat tails can be
broken down to provide energy.
Isomers
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 Isomers are compounds with the same molecular formula but different structures and
properties
Structural isomers have different covalent arrangements of their atoms
-For example: C6H12O6 is the molecular formula for glucose, fructose, and galactose.
Glucose and galactose are hexagons, but fructose is a pentagon and is sweeter than the others.

Geometric isomers have the same covalent arrangements but differ in spacial arrangements around a
Carbon-Carbon double bond
-Always around a C = C bond
-A cis isomer has the same atoms attached to double-bonded carbons on the same side of the
double bond
-A trans isomer has these atoms on opposite sides of the double bond.

Enantiomers are isomers that are mirror images of each other around an asymmetrical carbon
-An asymmetrical carbon is a carbon that is covalently bonded to four kinds of atoms or groups
of atoms, whose arrangement can result in mirror images
-They’re left and right handed versions of each other and can differ greatly in their biological
activity
-For example: Our hands are mirror images of each other.2 isomers are designated the L and D
isomers L for the left hand, D for the right hand. Enantiomers can’t be superimposed on each
other.

Characteristic chemical groups help control how biological molecules function

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 In an organic molecule, the chemical groups that attach to the carbon skeleton are essential to
the distinctive properties of the molecule
The Chemical Groups Most Important in the Process of Life
 Different chemical groups affect the molecules shape  This affects function!!
*So these important chemical groups are called functional groups
 For example: different steroids are created by attaching different functional groups to rings.
 sex hormones, testosterone and progesterone are similar in shape, but different in function.
-Both are steroids, organic molecules in the form of 4 fused rings.
-They only differ in the chemical groups attached to the rings.

-The body takes in cholesterol, which binds to the hormones.

Other examples = enzymes and antibodies. Their shape is essential because they have to fit into
special binding spots.

 The 7 most important chemical groups are listed below. The 1st 6 act as functional groups and
are hydrophilic, increasing solubility of compounds in water. But methyl is unreactive.

Structure Name of Compound

Hydroxyl Oxygen and hydrogen (–OH ) Alcohols (names usually end in –ol)

Example, ethanol

Carbonyl Carbon double bonded to an oxygen Aldehyde if carbonyl group is at the

end of the skeleton (-CHO, example
CO in glucose)
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Ketone if it’s in the middle,

example fructose

Carboxyl Carbon double bonded to an oxygen Carboxylic acids or organic acids

and bonded to an –OH group
They tend to release H+, becoming
-
–COOH a carboxylate ion (–COO )

Example, acetic acid

Amino A nitrogen atom bonded to 2 Amines

hydrogens
Can act as bases, picking up a
+
–NH2 hydrogen ion becoming –NH3

Example, amino acid glycine

Amide -CONH2 Amides are not basic but the most

polar functional group
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Sulfhydrl A sulfur atom bonded to a hydrogen Thiols

–SH Example, amino acid cysteine

Phosphate A phosphorus atom is bonded to 4 Organic phosphates

oxygen atoms: on oxygen is bonded to
the carbon skeleton, 2 oxygens carry Example, glycerol phosphate
negative charges

–OPO3 2--

Methyl A carbon bonded to three hydrogens Methylated compounds may have

their function modified due to the
–CH3 addition of the methyl group

Chapter 5
Organic compounds:
1) Carbohydrates
2) Lipids
3) Proteins
4) Nucleic acids

Macromolecules
 Carbohydrates, proteins, and nucleic acids are all macromolecules
 Polymers are chain-like molecules formed from the linking together of many similar or identical
small molecules called monomers.
 Monomers are the repeating units that serve as the building blocks of a polymer.
The Synthesis and Breakdown of Polymers
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 Condensation/dehydration reaction: the reaction in which 2 molecules are covalently bonded to

each other through loss of a water molecule
-monomers are connected through dehydration reactions
-One monomer contributes a hydroxyl group (—OH) and the other provides a hydrogen (—H)
-Enzymes are specialized macromolecules that catalyze both dehydration reactions and
hydrolysis.
 Hydrolysis: a process that breaks bond between monomers by adding a water molecule
-it’s the reverse of dehydration reactions
-A hydrogen from the water molecule attaches to one monomer, and the hydroxyl group
attaches to the other monomer
-For example: digestion
-organic material in our food is broken down, with the help of enzymes, through
hydrolysis

Carbohydrates
 Functions of carbohydrates:
1) Quick energy (4-5 calories per gram)
2) Structure and support (cellulose and chitin)
 Empirical formula for all carbohydrates= CH2O
-literally a carbon + a water molecule  a hydrated carbon molecule  a carbohydrate
-All carbohydrates contain C, H, and O
 Sugars may be aldoses or ketoses, depending on the location of the carbonyl group.
-Aldoses = aldehyde sugars = carbonyl group on the end of the molecule
-example: glucose and galactose
-Ketoses = ketone sugars = carbonyl group in the middle of the molecule
-example: fructose
 Sugars many also be classified according to the length of their carbon skeletons.
-The size of the carbon skeleton ranges from 3 to 7 sugars, with hexoses (C6H12O6 = glucose,
fructose, galactose), trioses, and pentoses found most commonly.
-Even though a fructose molecule has 5 sides, it is still a hexose because it has 6 carbons
 Sugar molecules may be enantiomers due to the spatial arrangements of parts around asymmetrical
carbons (like glucose and galactose- see figure 5.3)
 Most carbons form rings because it’s the most stable configuration
-Carbons are numbered 1 through 6: these numbers refer to their location

1) Monosaccharides
o Glucose

C6H12O6 o Fructose
o Galactose
*galactose is never found by itself
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-Same molecular formula, but different structural formulas  they’re structural isomers
-Glucose= major source of nutrition for cells
-It is broken down to yield energy in cellular respiration
2) Disaccharides
o Maltose = glucose + glucose
C12H22O11 o Sucrose = glucose + fructose
o Lactose = glucose + galactose
*Condensation/ Dehydration reactions:
-A glycoside linkage is a covalent bond between any 2 monosaccharides.
-Glycoside linkages form through dehydration reactions, when a water molecule is
removed (hydroxyl group is removed from one monosaccharide and a hydrogen is
removed from the other)
-Glycoside linkages form between different carbons depending on the monosaccharide:
-Glucose + glucose forms 1-4 glycoside linkages. (This means that Carbon 1 from
the 1st glucose is bonded to Carbon 4 from the other)
-Fructose + glucose forms 1-2 glycoside linkages
3) Polysaccharides
Polysaccharides are storage or structural macromolecules made from a few hundred to a few
thousand monosaccharides. They’re polymers of monosaccharides.
The two forms of glucose
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a. Starch = amylose
-unbranched
*found in plants
-1-4 alpha linkages: bonds are below the plane of the molecule

-We have enzymes that can digest alpha linkages

-These linkages give starch a helical shape
-Starch doesn’t dissolve in water. When you cook potatoes or pasta, they get soft
because you’re breaking glycoside bonds and getting the molecules to uncoil.
b. Cellulose
-1-4 beta linkages: bonds are alternative above the plane of the molecule

-So 1-4 linkages in amylose and cellulose have the same composition, but the
configuration of the ring form of glucose and the resulting geometry of the
glycosidic bonds are different

*We cannot digest cellulose because we do not have the enzymes needed to break
down cellulose
-Enzymes must fit their substrate, so different enzymes break down starch and
cellulose. We don’t have enzymes that can break down beta linkages.
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-Only a few organisms (some microbes and fungi) have enzymes that can digest
cellulose.
-Cows have enzymes from prokaryotes and bacteria that help them digest
cellulose. Bacteria make vitamin K that helps break it down.
-Foods with cellulose include fruits and vegetables – have natural sugars,
provide fiber in our diet, and fill you up more with fewer calories.
*Cellulose is the major component plant cell walls.
-Hydrogen bonds between hydroxyl groups hold parallel cellulose molecules
together to form strong microfibrils.
-It’s the most abundant organic compound on Earth
c. Glycogen
-highly branched and complex made from alpha glucose.
-Found in animals (often called animal starch)
-it’s stored in liver and muscle tissue as quick energy that’s readily available
*Short term energy storage
d. Amylopectin
-branched form of starch
-found in plants
-it has alpha linkages – we can digest it
e. Chitin
-structural polysaccharide formed from glucose monomers with a nitrogen-
containing group

-provides structure and support

-forms the exoskeleton of arthropods and the cell walls of many fungi
-We can’t break it down or get nutrients from it because it also has beta linkages

Lipids
-All lipids are hydrophobic
-long term storage of energy
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-Lipids are a more condensed and packed way to store energy, and they have more categories
 important to animals who are always on the move
-provides 9-10 cal per gram
-has the elements C, H, and O
-mostly consist of hydrocarbons
1) Triglycerides
 Glycerol + 3 Fatty acids  Triglyceride + 3H2O
-3 ester linkages = bond between glycerol and fatty acid

-This is a dehydration reaction: loss of a water molecule

-The carbonoxyl end of the fatty acid loses an – OH. The glycerol loses an – H.
-Fatty acids- consists of a long hydrocarbon chain with a carboxyl group at one end
 Fats are hydrophobic because the fatty acid chains are nonpolar
-The nonpolar hydrocarbons make it nonpolar
 Unsaturated fats:
-has double bonds
-fewer hydrogens per carbon
-healthy
-liquids at room temperature
-the cis double bonds create a kink in the hydrocarbon chain and prevents fat
molecules that contain unsaturated fatty acids from packing closely together
and becoming solidified and fixed
-The fats of fish and plants are generally unsaturated and are called oils
-examples: vegetable, olive, peanut, sunflower, and corn oils
 Saturated fats:
-only have single bonds
-unhealthy
-increases blood pressure and leads to heart disease
-solids at room temperature
-from animals
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o Trans fats are made in the process of hydrogenation: converting from unsaturated to
saturated fats to make the molecules solid
-extremely unhealthy and leads to heart disease
-example: oreos
 Functions of fats:
1) Excellent energy storage molecules
-Contains 2x the energy reserves of carbohydrates
2) Cushions organs and insulates the body
-example: adipose tissue, which is made of fat storage cells
2) Phospholipids
 Phospholipids consist of a glycerol linked to 2 fatty acids and a negatively charged phosphate
group, to which other small molecules are attached.
 Insoluble in water:
-phosphate head = polar
-phosphate group
-carries a large negative charge
-hydrophilic
-fatty acid tails tails = nonpolar
-fatty acids
-hydrophobic
 Function: STRUCTURE- they are the primary component in cell membranes:
-form the phospholipid bilayer
-regulates the types of material that move in and out of cells
-keeps animal cells flexible
Extacellular fluid =H20 outside of cell
nucleus cell membrane
Phospholipid
cytoplasm Bilayer

Hydrophilic head
Cell cytoplasm = H20 inside of cell
Hydrophobic tails The hydrophilic head turns outward towards
water. The hydrophobic tails turn inward
away from water.

3) Steroids
 4 fused carbon rings with attached groups
-Have a totally different structure – they’re only classified as lipids because of their
insolubility
-Typically come from animals
 Function: Many are hormones or pre-cursors to hormones
 Examples: cholesterol is an important steroid that is a common component of animal cell
membranes.
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-It is a pre-cursor for other steroids, including estrogen and testosterone. Cholesterol
molecules are modified to form sex hormones and can act as signaling molecules.
-Heart disease: too much cholesterol can lead to narrowed arteries and blocked blood
vessels, increasing blood pressure  This causes heart disease and atherosclerosis
-Structure: cholesterol increases the fluidity of cell membranes
 Are found in:
-Cholesterol - cell membranes
-Hormones – reproductive organs

Proteins
-Contain carbon, hydrogen, oxygen, and nitrogen (*carbs and lipids don’t have nitrogen)
Variety of Functions
1) Structural – provides structure and support.
-Keratin is the protein of hair, fur, claws, beak, nails.
-Actin and myosin are the proteins of muscle tissue, and are responsible for muscle
movement.
2) Enzymes – catalyze reactions
-Digestive enzymes like amylase catalyze the hydrolysis of polymers in food.
-break down (catabolism) or build up molecules (anabolism)
3) Transport – across cell membranes
-In red blood cells, hemoglobin transports oxygen from the lungs to other parts of the
body
4) Defense – protection against disease
-antibodies – combat bacteria and viruses
5) Storage – store energy
-Proteins in meat, egg white (protein = albumin), legumes, milk (protein =casein)
-provide 4-5 cal per gram of energy
6) Information receptors – response of cell to chemical stimuli
-Receptors on the cell surface of a nerve cell detect chemical signals released by other
nerve cells.
7) Hormones – signaling molecules that help with the coordination of an organism’s activities
-Insulin regulates concentration of sugar. Somatotropin is the protein in HGH (human
growth hormones).
Polypeptides
 A polypeptide is a polymer of amino acids.
 A peptide bond is a bond between amino acids.
-links the carboxyl group of one amino acid with the amino group of another
 A protein consists of one or more polypeptide chains folded into a specific 3-D shape

Amino Acid Structure:

variable group **Composed of an asymmetric carbon (called
the alpha carbon) bonded to a hydrogen, a
carboxyl group, an amino group, and a
variable side chain called the R group**
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R
amino H O carboxylic acid
group N–C–C group
H H OH

 At the pH in a cell, the amino and carboxyl groups are usually ionized.
 The R group is the variable group and it differs in different kinds of amino acids.
-It confers the unique physical and chemical properties of each amino acid.
-There are 20 different R groups.
-Side chains may be either nonpolar and hydrophobic, or polar and charged (acidic or basic) and
hydrophilic.
 Amino acids usually end in –ine
 20 different amino acids
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 Polypeptide chains are several amino acids linked by peptide bonds. Polypeptide chains have an
amino end (N-terminus) with a free amino group, and a carboxyl end (C-terminus) with a free
carboxyl group.

Protein Structure and function

 A protein has a unique 3-dimensional shape, or structure, created by the twisting or folding of
one or more polypeptide chains
 Protein structure depends on the interactions between the amino acids that make up the
polypeptide chain and usually arises spontaneously as the protein is synthesized in the cell
 The unique structure of a protein enables it to recognize and bind to other molecules

4 Levels of Protein Structure

1) Primary Structure
-The unique, genetically coded sequence of amino acids within a protein
-DNA encodes the sequence and determines how amino acids are put together
2) Secondary Structure
-Involves the coiling and folding of the polypeptide backbone
-An alpha helix = coils
-produced by hydrogen bonding between every 4th amino acids
-A beta pleated sheet = folds
-is also held by repeated hydrogen bonds along regions of polypeptide backbone lying
parallel to each other
-pleated sheets make up the core of many globular proteins
-This is stabilized by hydrogen bonds between the repeating constituent amino acids of the
polypeptide backbone
-Hydrogen bonds form between the electronegative oxygen of one peptide bond and
the weakly positive hydrogen attached to the nitrogen of another peptide bond
-The cell cytoplasm is made of water, so:
-The hydrophilic parts of the polypeptide chain turn outward
-The hydrophobic parts turn inward
3) Tertiary Structure
-Tertiary structure result from interactions between the various side chains (R groups) of the
constituent amino acids
-These interactions include:
-Hydrophobic interactions between nonpolar side groups clumped in the center of the
molecule due to their repulsion by water
-Van der Waals interactions among those nonpolar side chains (very weak)
-Hydrogen bonds between polar side chains
-Ionic bonds between negatively and positively charged side chains
*These interactions produce the stable and unique shape of the protein
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-Strong covalent bonds, called disulfide bridges, may reinforce the protein’s structure
-may occur between the sulfhydryl side groups of cysteine monomers that have been
brought closer together by the folding of the polypeptide

4) Quaternary structure
-2 or more polypeptide subunits combine and interact with each other
-occurs in proteins that are composed of more than one polypeptide chain
-the individual polypeptide subunits are held together in a precise structural arrangement
-For example: In hemoglobin proteins, each subunit has a nonpolypetpide component
called a heme, with an iron atom that binds oxygen

Proteins can change shape

 Folding of polypeptides normally occurs as the protein is being synthesized within the cell. However,
protein conformation also depends on the physical and chemical conditions of the protein’s
environment.
 Denaturation is a change in original protein shape, usually resulting from a change in the pH,
temperature, salt concentration, or exposure to chemicals
-Because it is misshapen, the denatured protein is biologically inactive
-Most proteins become denatured if they’re transferred form an aqueous environment to an
organic solvent.
 If a denatured protein remains dissolved, it can often renature when the chemical and physical
aspects of its environment are restored to normal

Defective Proteins
-a problem with encoding DNA can have serious effects on protein shape and function
Sickle cell anemia
-Results from a simple change in the primary level in 1 amino acid
-called a point mutation, resulting from substitution
-This changes the shape of the secondary and tertiary levels too  the hemoglobin protein is misshapen
Muscular dystrophy
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-defective protein within muscle (actin/myosin)

Tay-Sachs
-enzymes are defective
Hemophilia
-clotting protein is defective
Cystic fibrosis
-transmembrane protein is defective (Cl—ions)

Nucleic Acids
-information molecules that carry genetic code
DNA
-is inherited from one generation to the next and is copied whenever a cell divides so that all cells of an
organism contain its DNA
-polymer of nucleotides
-nucleotide:
1. 5-carbon sugar (deoxyribose)
2. Phosphate group
3. Nitrogenous base
-Adenine
-Thymine (*Only in DNA)
-Guanine
-Cytosine
-found in the nucleus in chromosomes

RNA
-directs protein synthesis
-polymer of nucleotides
-nucleotide:
1. 5-carbon sugar (ribose)
2. Phosphate group
3. Nitrogenous base
-Adenine
-Uracil (*Only in RNA)
-Guanine
-Cytosine
-found throughout the cell
-in the nucleus (mRNA), in ribosomes (rRNA), and as transport (tRNA)
 22

Structure of Nucleic Acids

 Polynucleotides are polymers of nucleotides—monomers that consist of a pentose (5-carbon
sugar), a phosphate group, and a nitrogenous base
 A monomer without the phosphate group is called a nucleoside
 There are 2 types of nitrogenous bases:
1. Pyrimidines= 6-membered rings of carbon and nitrogen
-cytosine (C), thymine (T), and uracil (U)
2. Purines = add a 5-membered ring of carbon and nitrogen to the pyrimidines ring
-adenine (A) and guanine (G)
 Covalent bonds between sugar, phosphate and the base
 Hydrogen bonds between nitrogenous bases
-Easily broken
 Phosphodiester linkages = covalent bonds between nucleotides
-Between the sugar of one nucleotide and the phosphate of the next
-This bonding results in a sugar-phosphate backbone with repeating sugar and phosphate units
 The polymer has 2 distinct ends: a 5’ end with a phosphate attached to a 5’carbon of a sugar and a
3’ end with a hydroxyl group on a 3’ sugar
-The nitrogenous bases extend from this backbone of repeating sugar-phosphate units
-The unique sequence of bases in a gene codes for the specific amino acid sequence of a protein
 23

Chapter 6
Levels of Organization
 Biosphere
 Biome
 Ecosystem
 Community
 Population
 Organisms
 Organ systems
 Organs
 Tissues
 Cell- basic unit of life
 Organelles
 Molecules
 Atoms (basic unit of matter)
5 Kingdoms of Life
1) Animals
2) Plants
3) Protists
4) Fungi
5) Bacteria

Prokaryotes vs. Eukaryotes

All cells are bounded by a plasma membrane which encloses a semifliud medium called cytosol. All cells
contain chromosomes and ribosomes.
Prokaryotes Eukaryotes
-Bacteria -Protist
*No membrane bound nucleus -Fungi
-Nucleoid: the DNA of prokaryotic cells is -Animal
concentrated in this region – in single loops -Plant
*No organelles *Has a membrane-bound nucleus
*Has organelles
Cell Theory
1) The cell is a basic unit of life.
2) Cells come from preexisting cells.
3) All living things are made of cells.
Cytosol is the watery basis in which organelles are suspended in; it’s also the interior of a prokaryote cell
Cytoplasm is cytosol + organelles
The plasma membrane surrounding every cell must provide sufficient surface area for exchange of
oxygen, nutrients, and wastes relative to the volume of the cell
-Small cell size is due to geometry and the requirements of metabolism
 24

-The smaller the cell, the bigger the surface area to volume ratio
-Smaller cells are more beneficial:
1) More efficient diffusion of nutrients
2) More reproduction and healthier cells
3) Better chances of survival
The surface area to volume ratio becomes less favorable as a cell increases in size. The total volume
grows proportionally more than the surface area. Since a cell acquires resources through the plasma
membrane, cell size is limited.
The Structure of the Cell
Organelle and Function Cell type Location

Nucleus – contains instructions for making proteins Eukaryote Within cytosol,

usually centrally
Nuclear envelope- double membrane of phospholipids
located
and proteins surrounding the nucleus

Nuclear pores- small pores in the nuclear envelope that

regulate the exchange of materials between the
cytoplasm and the nucleus (DNA stays; RNA leaves)

Chromosomes- contain and carry genetic information in Eukaryote and In an eukaryote

the form of DNA; it’s chemistry is DNA prokaryote cell: in the nucleus
in single strands
Chromatin- material consisting of DNA and proteins
used for wrapping and packaging the DNA. In a prokaryote
Chromosomes are wrapped around histone proteins. cell: in the
Individual chromosomes are only visible in a dividing nucleoid in a
cell. single loop

DNA- the nucleic acid that makes up chromosomes

Gene- more specific bits of genetic information

Nucleoid- a region where the cell’s genes are located Prokaryote In the cytosol
on a single loop chromosome; same chemistry of DNA,
but not a membrane-bound nucleus like eukaryotic cells

Nucleolus- contains RNA that is used to make Eukaryote In the nucleus

ribosomes; not membrane bound so it will disperse and
“disappear” during meiosis and then recollect

Ribosomes- manufacture proteins; made of rRNA and Eukaryote and Free in the cytosol
proteins; made of 2 parts= large subunit and small prokaryote or bound to the
subunit rough ER and
 25

-Free ribosomes = make proteins that are used inside of nuclear

the cell; float free in the cytosol membrane

-Bound ribosomes= make proteins that are included

within membranes, packaged into organelles, or
secreted and used outside of the cell, like hormones
and antibodies; bound to rough ER or nuclear envelope

*Where the primary structure of proteins is made

Rough Endoplasmic Reticulum- modifies polypeptides Eukaryote Continuous with

by folding and coiling them into their normal shape the nuclear
(secondary shape); has ribosomes membrane

-Attaches carbohydrate chains (glycoprotein) which act

as markers or signals telling the protein where to go

-The packaged proteins leave the ER through vesicles

(and go to the Golgi Apparatus)

-It also manufactures membranes for the cell. Enzymes

built into the membrane assemble phospholipids, and
membrane proteins formed by bound ribosomes are
inserted into the ER membrane. Transport vesicles
transfer ER membrane to other parts of the cell.

*Where the secondary structure of proteins is made

Smooth Endoplasmic Reticulum- has 4 major functions: Eukaryote Continuous with

nuclear
1) Synthesis of lipids (phospholipids and steroids) membrane; in
2) Metabolism of carbohydrates in the liver cytosol

3) Detoxification of drugs and poisons, like

alcohol, aspirin, and antibiotics (Drugs increase
the liver’s production of smooth ER, leading to an
increased tolerance of these and other drugs)

4) Stores calcium ions in muscle cells (which is

called the sarcoplasmic reticulum)

Transport vesicles- membrane-bound sacs that pinch Eukaryote Pinch off

off the Golgi apparatus and transport substances membranes
outside of the cell; ID tell the vesicles where to go
 26

-Vesicles also pinch off from the ER and integrate into

the cis face of the Golgi apparatus, transporting
secretory proteins or ones for the membrane

Golgi apparatus- products of the ER are further Eukaryote In cytosol, further

modified, stored, and shipped to other destinations away from
nucleus
1) Carbohydrate chains are removed or
substituted cis face- “receiving”
side where vesicles
2) Secretes specific polysaccharides in plant cells from the ER join
(like pectin)
trans face-
3) Products are sorted by adding phosphate “shipping side”
groups as ID tags where vesicles
pinch off and leave
*Where the tertiary and quaternary structure is made

Lyosomes – membrane-enclosed sacs containing Eukaryote- only In cytosol

hydrolytic enzymes which speed up hydrolysis in animal cells
(breaking down and digesting macromolecules);
Lysosomes provide an acidic pH for these enzymes.

-Can be involved in:

1. Autodigestion- cells digest themselves

2. Apoptosis- programmed cell death (Example:

tadpoles are broken down and used to form
new cells in the form of frogs )

3. Phagocytosis- white blood cell engulfs food

into a food vacuole which fuses with lyosomes
and breaks it down

4. Autophagy- engulfs its own damaged

organelles

Peroxisomes – membrane enclosed sacs that break Eukaryote – In cytosol

down fatty acids to be sent to mitochondria for fuel and plants and
detoxify alcohol by transferring hydrogen from the animals
poison to oxygen to form hydrogen peroxide.

Contractile vacuole- pump out excess water from Eukaryote- In cytosol

freshwater protists so they don’t lyse (=burst) protists, plants,
 27

fungi

Central vacuole with tonoplast (water vacuole)– Eukaryotes –

surrounded by a vacuolar membrane (=tonoplast); plants, fungi,
stores organic compounds and inorganic ions; holds some protists
water and dissolves materials until it’s full of water  it
exerts turgor pressure, pushing the membrane against
the cell wall and increasing the cell size

*Turgor pressure causes plants to become turgid, rigid,

and expanded

Mitochondria- carry out cellular respiration and Eukaryotes In cytosol

produces ATP; has a folded double membrane, with (prokaryotes carry
out cellular
DNA and ribosomes that direct the synthesis of proteins
respiration, but
don’t use
C6H12O6 + O2  H2O + CO2 + ATP (energy)
mitochondria)

Choloroplasts- carry out photosynthesis and produce Eukaryotes – In cytosol

glucose; has a stacked double membrane; contain plants, algae,
chlorophyll and some
protists
6H2O + 6CO2  C6H12O6 + 6O2

*Allows organisms to manufacture their own food

Cell wall- provides structure and support; maintains cell Prokaryotes and Outer layer of the
shape and protects the cell from mechanical damage; Eukaryotes cell (outside the
made of cellulose, other polysaccharides, and proteins (plants, fungi, cell membrane)
and some
Plant cell walls = cellulose protists)
Fungi = chitin

Bacteria = peptidoglycan (sticky material made of protein

and sugar)

Cytoskeleton – network of protein fibers that consist of Eukaryotes Extends

different sizes throughout the
cytoplasm
Functions:

1) Reinforces the cell’s shape lk;kaf;lksjfla;sldkfja;slda;s

2) Transmits signals from the cell’s surface to its interior
3) Organizes cell’s structures and activities and helps to
move organelles within cells by interacting with motor
 28

proteins

*Cytoplasmic streaming is when the cytoskeleton

directs the movement of the cytoplasm by providing
the tracts. It’s more efficient in smaller cells

Microtubules – larger protein fibers made up of the Eukaryotes In the

protein tubulin that make up the cytoskeleton; example cytoskeleton
= centrioles in animal cells. Microtubules serve as tracks
along which organelles equipped with motor molecules
can move. They also separate chromosomes during
mitosis and meiosis (forming the spindle) and are the
structural components of cilia and flagella. Though
different in length, number per cell, and beating
pattern, cilia and flagella share a common
ultrastructure. They have nine pairs of microtubule
surrounding a central core of two microtubules. This
arrangement is referred to as “9+2” pattern.

Microfilaments – smaller protein fibers that make up Eukaryotes In the

the cytoskeleton. When coupled with motor molecule cytoskeleton
myosin, microfilaments can be involved in movement.
Example, amoeboid movement, cytoplasmic streaming,
and contraction of muscle cells.
*Actin and Myosin are important microfilaments in
muscle proteins

Intermediate filaments – permanent fixtures in cells Eukaryotes In the

responsible for maintaining shape and fixing position of cytoskeleton
certain organelles.

Extracellular matrix- made of protein fibers and Eukaryotes Outside of the cell
carbohydrates; is the “glue” that holds cells together (between cells)

Plasmodesmata- channels within plant cells that allow Eukaryotes – Between cells
connections between adjacent cells (water, small solutes, *plasmodesmata (they all help hold
and proteins and RNA can move throughout these channels) are only in cells together)
plants
Tight junction- where cell membranes are tightly
pressed together; creates a continuous seal that *the 3 junctions
prevents leakage are only in
animal cells
Desmosomes (anchoring junctions)- fastens cells
 29

together in strong sheets

Gap junctions (communicating junctions)- provides

cytoplasmic channels and allows communication
between cells

Cilia – shorter; numerous Eukaryotes and Outside cell,

prokaryotes found in
Flagella – long; usually single reproductive cells

Cell’s job = to make proteins

-Plasma membrane- controls transport of materials in/out of the cell
-Endomembrane system- consists of the nuclear envelope, ER, Golgi apparatus, lysosomes, vacuoles,
and the plasma membrane.
-The ER encloses a network of interconnected tubules or sacs called cisternae.
-As membranes move from the ER to the Golgi and then to other organelles, their compositions,
functions, and contents are modified
*These membranes are all related through direct contact or by the transfer of membrane
segments by the membrane-bound sacs called vesicles
-Mitochondria = makes ATP
-Chloroplasts = makes glucose in plants

Endosymbiant Hypothesis
-Eukaryotes came about from bacteria that have ingested other bacteria, where the ingested bacteria
became mitochondria and chloroplasts
-Both mitochondria and chloroplasts have double membranes and their own DNA
-mDNA = mitochondrial DNA that always comes from maternal DNA

Animal cells vs. Plant cells

Animal cells: Plant cells:
-Lysosomes (suicide sacs) -Chloroplasts (make glucose  can make their
-Centrioles (move chromosomes) own food)
-Flagella (in some plant sperm) -Central vacuole and tonoplast (get rid of excess
water)
-Cell wall (provide structure and support)
-Plasmodesmata (hold plant cells together)
 30

Chapter 7
 The plasma membrane is selectively permeable, allowing some materials to cross it more easily
than others and enabling the cell to maintain a unique internal environment
Cell Membranes are fluid mosaics of lipids and proteins
-According to the fluid mosaic model, the structure of membranes consists of various proteins
embedded in a phospholipid bilayer
-The structure of all membranes is similar
Cell Fluidity
 Membranes are held together primarily by weak hydrophobic interactions that allow the lipids and
some of the proteins to drift laterally
-Some membrane proteins seem to be held rigid by attachments to the cytoskeleton; others
appear to be directed in their movements by cytoskeletal fibers
 Phospholipids with unsaturated hydrocarbon tails maintain membrane fluidity at lower
temperatures
-The double bonds in the unsaturated fatty acid chains create a kink in the molecule, so it’s fluid,
not fixed
 The steroid cholesterol can be embedded in the membrane which also adds fluidity to the cell
-It prevents the close packing of lipids and enhances fluidity at lower temperatures
-Cholesterol is common in plasma membranes of only animals
-However, at WARMER TEMPERATURES, it restricts movement of phospholipids and reduces
fluidity
Transport Proteins
 Integral proteins extend throughout the entire membrane
-Also called transmembrane proteins
-Have 2 hydrophilic ends and a hydrophobic midsection that consists of one or more alpha
helical stretches of hydrophobic amino acids
 Peripheral proteins attached to the surface of the membrane, often to integral proteins
-Attachments of these membrane proteins to the cytoskeleton or extracellular matrix provide a
supportive framework for the plasma membrane
Membrane Carbohydrates
 Act as cell markers and cell receptors and help cells distinguish other cells
 The glycolipids and glycoproteins attached to the outside of plasmamembranes vary from cell to cell
-Glycoproteins are proteins with a glucose chain attached to it
-Glycolipids consist of a glucose chain attached to a lipid
Synthesis and Sidedness of Membranes
 Membranes have distinct inner and outer faces, related to the composition of the lipid layers, the
directional orientation of their proteins, and their attachment of carbohydrates to the extracellular
surface
 31

 Carbohydrates are attached to membrane proteins as they are synthesized in the ER and are
modified in the Golgi. Carbohydrates are also attached to lipids in the Golgi.
-When transport vesicles fuse wit the plasma membrane, these interior glycoproteins and
glycolipids become located on the extracellular face of the membrane

Membrane structure results in selective permeability

 The plasma membrane permits a regular exchange of nutrients, waste products, oxygen, and
inorganic ions.
 Biological membranes are selectively permeable; the ease and rate at which small molecules pass
through them differ
The Permeability of the Lipid Bilayer
 Hydrophobic, nonpolar molecules, such as hydrocarbons, CO2, and O2, can dissolve in and cross a
membrane
Transport Proteins
 Ions and polar molecules may move across the plasma membrane with the aid of transport proteins
 Functions of membrane proteins:
o Transport
-moving materials across the membrane
-can be either passive or active
o Enzymatic activity
-something binds to a protein outside and causes a change inside the cell
o Signal transduction
-something binds to a protein outside and causes a series of changes inside cell
o Cell-cell recognition
-some glycoproteins serve as ID tags that are recognized by other cells
o Intercellular joining
-membrane proteins of adjacent cells make attach in various kinds of junctions
o Attachment to the cytoskeleton and ECM
-Proteins attached to cytoskeleton = maintain internal support
-Proteins attached to the ECM = coordinate extracellular changes
 2 types of transport proteins:
1. Channel proteins – have a hydrophilic channel that certain molecules can enter and use
as a tunnel
a. Aquaporins = channel proteins that facilitate the passage of water
2. Carrier proteins- physically binds and transports a specific molecule and can change
shape
-It’s a more specific type of transport across the membrane

What determines how a molecule moves through the membrane?

Passive transport:
 32

 High concentration to low concentration

 With the concentration gradient
 No cellular energy
 Uses the kinetic energy of molecules
 3 types of passive transport:
1) Diffusion- the movement of a substance down its concentration gradient due to random
thermal motion
-The diffusion of one solute is unaffected by the concentration gradients of other
solutes
-The cell doesn’t expand energy when substances diffuse across membranes
-small, hydrophobic molecules like N2, O2, CO2, CO move through the membrane
by diffusion
-small uncharged molecules like glycerol, ethanol, and ether move through the
membrane by diffusion

2) Osmosis- the diffusion of water across a selectively permeable membrane

-water diffuses down its own concentration gradient, which is affected by the solute
concentration
-When there is more solute particles, more water molecules bind to them. This
lowers of water that’s free to cross the membrane
-water diffuses through the membrane by osmosis, with the help of aquaporins

3) Facilitated diffusion- diffusion across the membrane with the help of transport proteins,
either channel or carrier proteins
-Many ion channels are gated channels, which open or close in response to
electrical or chemical stimuli
-small polar molecules like glucose, amino acids, and nucleotides diffuse through
the membrane with the help of proteins

Small hydrophobic molecules

Passive
Small uncharged molecules Transport

Water (through aquaporins)

Small polar molecules

Channel protein

Small, highly charged particles (ions)

Active
Carrier protein Transport
(aka protein pump)
 33

Active transport:
 Low concentration to high concentration
 Against the concentration gradient
 Requires ATP
 Uses transmembrane proteins
 4 types of active transport:
1) Proton pump
-moves H+ ions across the membrane through carrier proteins
-An H+ ion is a proton
-transport within an organelle, like cellular respiration
2) Cotransport
-Transporting 2 solutes across the membrane when the active transport of a 2nd solute is
indirectly driven by the ATP-powered pump that drives the transport of the 1st
-For example:
-H+ ions move out of the cell through a protein.
-This changes the pH, making the extracellular fluid more acidic, and creates an
electrochemical gradient. A change in pH can change protein shape.
-H+ ions then diffuse back in, but now sucrose molecules can move in as well,
through proteins that changed shape.
3) Sodium-potassium pump
-Exchanges Na+ (sodium ion) for K+ (potassium ion) across the plasma membrane of
animal cells
-This transport involves ATP and special proteins that can change shape
-This is how it works:
-Na+ ions move through a protein  When ATP binds to the protein in order to
help the Na+ ions go through, the protein changes shape (the shape that
matches K+ ions)
-Now K+ ions can go through the membrane.  When ATP binds to the protein
in order to help the K+ ions go through, the protein changes shape again (the
shape that matches Na+ ions)
-Now Na+ ions can go through the membrane again.
-It creates a higher concentration of potassium ions and a lower concentration of sodium
ions within the cell.
-It creates membrane potential, a voltage difference across a membrane due to
unequal distribution of positive and negative ions.
-An ion diffuses down its electrochemical gradient, which is created by charged
particles moving across the membrane.
4) Receptor-mediated endocytosis
-A specific type of endocytosis: brings in specific macromolecules that have to bind with
receptors on the inside of the membrane in order to be transported
-Doesn’t use proteins, but does use ATP
 34

Bulk transport across the plasma membrane occurs by exocytosis and

endocytosis
Bulk transport requires ATP to transport larger biological molecules, packaged in vesicles, across the
membrane. But it doesn’t use proteins.
Exocytosis
-In exocytosis, the cell brings out and secretes large molecules by the fusion of vesicles with the
plasma membrane
Endocytosis
-Endocytosis is when the cell takes in molecules by forming vesicles from the plasma membrane
-A region of the plasma membrane sinks inward and pinches off to form a vesicle that
contains materials that had been outside the cell
-3 types of endocytosis:
1) Phagocytosis = cellular eating (bringing in solids)
-The vesicle then fuses with lysosomes containing hydrolytic enzymes in order
to be digested
2) Pinocytosis = cellular drinking (bringing in liquids)
3) Receptor mediated endocytosis (see above)

Hypertonic and Hypotonic

Hypertonic solution: high solute, low water
Hypotonic solution: low solute, high water
Isotonic solution: the same amount of solute

-Protists like paramecium are often hypertonic to their environment. (This means that they have less
water and more solute compared to their environment)
-The direction of water movement is from high to low, so water diffuses from the outside to the
inside of the cell.
-However, Paramecium will not burst because they have contractile vacuoles that can pump out
excess water

Onion Cell:

Cell wall 96% water

Environment: distilled
Cell membrane Hypertonic
water ( 100%) = Hypotonic
Water vacuole
Nucleus Water flows in

An onion cell placed in a hypotonic environment is hypertonic relative to

its environment  water flows in
-The cell membrane is pressed against the cell wall
*It was high turgor pressure, so the cells are turgid and rigid.
-Only cells with cell walls can have turgor pressure
 35

96% water
Environment: 15% solute
Hypotonic
(85% water) = Hypertonic

Water flows out

An onion cell placed in a hypertonic environment (higher solute, lower water) is hypotonic
(lower solute, higher water) relative to its environment.  water flows out
-The cell membrane shrivels and shrinks
-The cell loses turgor pressure
**This is called plasmolysis: the loss of cytoplasm and water from the cell
 Can cause plants to wilt and die
Red blood cell:
If placed in distilled water:
-The red blood cell would be hypertonic relative to its environment which would be hypotonic
(It would have more solute and less water than distilled water.)
-So water would flow INTO the cell.
-Red blood cells are animal cells, so they do not have a cell wall.  If too much water flows in,
the red blood cell would lyse, or burst and explode.
If placed in 15% solute:
-The red blood cell would be hypotonic relative to its environment which would be hypertonic
(It would have less solute and more water than its environment.)
-So water would flow OUT of the cell.
-If too much water flows out, the red blood cell would shrivel up and die.

Tonicity
 Tonicity is the tendency of a cell to gain or lose water and is affected by the relative concentrations
of solutes that cannot cross the membrane in the solution and in the cell
 Isotonic solution:
-An animal or a plant cell will neither gain nor lose water in an isotonic environment
-A plant cell in an isotonic environment is flaccid.
 Hypertonic solution:
-An animal cell will gain lose water and shrivel.
-A plant cell undergoes plasmolysis, the pulling away of the plasma membrane from the cell wall
as water leaves and the cell shrivels.
 Hypotonic solution:
-An animal cell will gain water, swell, and possibly lyse (burst).
-A plant cell will gain water, swell against its cell wall, and become turgid.
-Turgid cells provide mechanical support for nonwoody plants
 Cells without rigid walls must either live in an isotonic environment, such as salt water or isotonic
body fluids, or have adaptations for osmoregulation, the control of water balance.
 36

Water potential is the potential energy of water per unit volume. It is also called free energy per mole
of water. Water moves from an area of higher water potential or higher free energy to an area of lower
water potential or lower free energy.

 = P + S
Or
Water potential = pressure potential + solute potential
Solute Potential  S - Measure of the tendency of water to move into a region due to the presence of
solutes. Solutes bind water molecules reducing the number of free water molecules which lowers
waters ability to do work.

 S of pure water is 0.  S of any solution at atmospheric pressure is always negative because there are
less free water molecules to do work.
Solute potential = osmotic potential
Pressure Potential P - measure of physical (hydrostatic) pressure on a solution exerted by cell walls.

Turgor pressure is the pressure exerted by water on the

plant cell wall.

Pressure potential = Turgor pressure

Pressure potential for cells at atmospheric pressure is 0.

 37

Plant Cell when placed in hypotonic solution becomes turgid and attains equilibrium

Turgid is normal plant cell and isotonic is normal animal cell

 38

Plants transport water by maintaining positive potential in gradient form by changing concentration of
solutes in their cytoplasm. The cells mostly have low water potential compared to surrounding solution
causing water to move in to the cell.