BIO152

Lecture 3: Water, Carbon, and Macromolecules

PPT Lectures by

Sept. 17, 2013

Prof. Rawle
@FiRawle

Stephanie Scher Pandolfi

and Sharon Gillies

#BIO152
2014 Pearson Canada, Inc.

Announcements
Evolution survey now available on Blackboard.
Please note these slides are summary slides of chapters

2 and 3 in your text. We will not be covering all of these

slides in class, but you are expected to know this material.
Most of this material should be review from high school.

Ch 2: Key Concepts
Molecules form when atoms bond to each other. Chemical bonds are
based on electron sharing. The degree of electron sharing varies from
nonpolar covalent bonds to polar covalent bonds to ionic bonds.
Water is essential for life. Water is highly polar and readily forms
hydrogen bonds. Hydrogen bonding makes water an extremely
efficient solvent.
Energy is the capacity to do work or supply heat, and can be (1) a stored
potential or (2) an active motion. Chemical energy is a form of potential
energy, stored in chemical bonds.
Chemical reactions tend to be spontaneous if they lower potential energy
and increase entropy (disorder). An input of energy is required for
nonspontaneous reactions to occur.
Most of the important compounds in organisms contain carbon. Key
carbon containing molecules formed early in Earths history.

Basic Atomic Structure

Atoms are composed of:
Protons positively charged particles
Neutrons neutral particles
Electrons negatively charged particles
Protons and neutrons are located in the nucleus.
Electrons are found in orbitals surrounding the nucleus.

Elements The Building Blocks of Chemical Evolution

Every different atom has a characteristic number of protons in

the nucleus, called the atomic number.

Atoms with the same atomic number have the same chemical

properties and belong to the same element.

The mass number is the number of protons + neutrons of the

most common isotope.

Forms of an element with different numbers of neutrons are

isotopes.

Electron Arrangement around the Nucleus

Electrons move around atomic nuclei in specific regions called

orbitals.
Each orbital can hold up to two electrons.

Orbitals are grouped into levels called electron shells.

Electron shells are numbered, with smaller numbers closer

to the nucleus.
The electrons in the outermost shell are called valence
electrons.

Elements commonly found in organisms have at least one

unpaired valence electron. The number of unpaired electrons in

an atom is its valence.

Chemical Bonding
Unfilled electron orbitals allow formation of chemical bonds,

and atoms are most stable when each electron orbital is filled.
Covalent bond: Each atoms unpaired valence electrons are shared by

both nuclei to fill their orbitals.

Ionic bond: Electrons are transferred from one atom to another.
Substances held together by ionic or covalent bonds are called molecules.

Covalent Bonds
Electrons are not always shared equally. An atom in a molecule

with a high electronegativity will hold the electrons more

tightly and have a partial negative charge (), whereas the
other atom will have a partial positive charge (+).
Differences in electronegativity dictate how electrons are

distributed in covalent bonds.

Nonpolar covalent bond: Electrons are evenly shared between two atoms

and the bond is symmetrical.

Polar covalent bond: Electrons are asymmetrically shared.

Ions and Ionic Bonds

An atom or molecule that carries a charge is called an ion.
Cation: An atom that loses an electron and becomes positively charged.
Anion: An atom that gains an electron and becomes negatively charged.
The resulting attraction between oppositely charged ions is an

ionic bond.

The Electron-Sharing Continuum

The degree to which electrons are shared in chemical bonds
forms a continuum, from equal sharing in nonpolar covalent
bonds, to unequal sharing in polar covalent bonds, to the
transfer of electrons in ionic bonds.

How Many Bonds Can an Atom Have?

The number of unpaired electrons determines the number of

bonds an atom can make.

Atoms with more than one unpaired electron can form multiple

single bonds or double or triple bonds.

Figure 2.9 The Geometry of Methane and Water.

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Representing Molecules
The shape of a simple molecule is governed by the geometry of

its bonds.
Molecular formulas indicate the numbers and types of atoms

in a molecule (e.g., H2O, CH4).

Structural formulas indicate which atoms are bonded together

and whether the bonds are single, double, or triple bonds.

Ball-and-stick models and space-filling models show 3D

geometry.

Chemical Reactions
Chemical reactions occur when:
1. One substance is combined with another.
Atoms are rearranged in molecules, or small molecules combine to form larger

molecules.
2. One substance is broken down into another substance.
Molecules are split into atoms or smaller molecules.

In most cases, chemical bonds are broken and new bonds form.

Quantifying Molecules
The molecular weight of a molecule is the sum of the mass

numbers of all the atoms in the molecule.

One mole, or 6.022 1023 molecules, has a mass equal to the

molecular weight expressed in grams.

The concentration of a substance in a solution is typically

expressed as molarity (M), which is the number of moles per

liter.

Why Is Water Such an Efficient Solvent?

Life is based on water because water is a great solvent.
The covalent bonds in water are polar because oxygen has a

greater electronegativity than hydrogen.

Oxygen has a partial negative charge.
Hydrogen has a partial positive charge.

Hydrogen bonds are the weak electrical attractions between the

partially negative oxygen of one water molecule and the partially

positive hydrogen of a different water molecule.
Can also form between a water molecule and another polar molecule.

Water and Hydrogen Bonds

Ions and polar molecules stay in solution because of their

interactions with waters partial charges. These atoms and

molecules are said to be hydrophilic.
Uncharged and nonpolar compounds do not dissolve in water

and are said to be hydrophobic.

Hydrogen bonding makes it possible for almost any charged or

polar molecule to dissolve in water.

Correlation of Waters Structure and Properties

Water is unique due to its small size, bent shape, highly polar

covalent bonds, and overall polarity.

Water also has several remarkable properties, largely due to its

ability to form hydrogen bonds. Water is:

1.
2.
3.
4.

Cohesive
Adhesive
Denser as a liquid than a solid
Able to absorb large amounts of energy

A Closer Look at the Properties of Water

Cohesion binding between like molecules
Results in high surface tension
Adhesion binding between unlike molecules
Water expands as it changes from a liquid to a solid.
This is why ice floats!
Water has an extraordinarily large capacity for absorbing heat.
High specific heat
High heat of vapourization

AcidBase Reactions and pH

Proton [hydrogen ion (H+)] concentration is the basis of the pH

scale.
pH expresses proton concentration in a solution.

The pH of pure water is 7.

Acids have a pH of less than 7.
Bases have a pH of greater than 7.
In acidbase reactions, a proton donor (acid) transfers a proton

to a proton acceptor (base).

The pH Scale and Buffers

The pH scale is logarithmic:
pH = log [H+]
Greater H+ concentration lower pH more acidic
Lower H+ concentration higher pH more basic/alkaline
Buffers are compounds that minimize changes in pH.

Chemical Evolution Theory

Simple molecules present on ancient Earth reacted to create

larger, more complex molecules.

This may have happened in:
The atmosphere
Deep-sea vents

How Do Chemical Reactions Happen?

Chemical reactions have reactants and products. For

example:
CO2(g) + H2O(l) H2CO3(aq)
Chemical equilibrium occurs when the forward and reverse

reactions proceed at the same rate and the quantities of reactants

and products remain constant.
Endothermic reactions must absorb heat to proceed, but

exothermic reactions release heat.

What Is Energy?
Energy is the capacity to do work or supply heat. This capacity
exists in one of two waysas a stored potential or as an active
motion.

Potential Energy and Kinetic Energy

Stored energy is called potential energy. An objects position

determines its ability to store energy. For example:

Electrons in an outer shell (farther from the positively
charged nucleus) have more potential energy than do
electrons in an inner shell.
The energy of movement is called kinetic energy or thermal

energy, which is measured as temperature.

Low-temperature objects have slower molecules than high-temperature

objects.

Heat and the First Law of Thermodynamics

Heat is the thermal energy transferred between objects of different

temperatures.

The first law of thermodynamics states that energy is

conservedit cannot be created or destroyed, but it can be

transferred or transformed.

What Makes a Chemical Reaction Spontaneous?

Chemical reactions are spontaneous if they proceed on their

own, without any continuous external influence such as added
energy.

The spontaneity of a reaction is determined by two factors:

1. The amount of potential energy
Products of spontaneous reactions have less potential energy than the reactants.
2. The degree of order
Products of spontaneous reactions are less ordered than the reactants.

The Second Law of Thermodynamics

Entropy (S) is the amount of disorder in a group of molecules.
The second law of thermodynamics states that entropy always

increases.
In other words, chemical reactions result in products with less ordered

(usable) energy.

In general, physical and chemical processes proceed in the

direction that results in lower potential energy and increased

disorder.

Gibbs Free-Energy Change

The Gibbs free-energy change (G) determines whether a

reaction is spontaneous or requires energy.

G < 0 is an exergonic spontaneous reaction.
G > 0 is an endergonic reaction that requires energy
input.
G = 0 is a reaction that is at equilibrium.

Temperature and Concentration Affect Reactions

Breaking and forming bonds depends on collisions between

substances.
This allows electrons to interact.

The rate of a reaction depends upon the number of collisions.

The number of collisions is dependent on the temperature and

concentration of the reactants:

Higher temperature more collisions faster reaction
Higher concentration more collisions faster reaction

Energy Inputs and the Start of Chemical Evolution

Formation of formaldehyde (H2CO) and hydrogen cyanide

(HCN) is the first step in chemical evolution and requires

energy input.
Photons are packets of light energy emitted by the Sun.
High-energy photons can break molecules apart by knocking

electrons away from valence shells. The resulting free radicals

have unpaired electrons and are extremely unstable and highly
reactive.

Chemical Energy Is a Form of Potential Energy

Significant amounts of H2CO and HCN could form under the

temperature and concentration conditions that were likely on

ancient Earth.
These products have more potential energy than the reactants.

Potential energy stored in chemical bonds is called chemical

energy.
Thus: solar energy (energy of the Sun) was converted into

chemical energy (in H2CO and HCN).

The Importance of Carbon

Carbon has great importance in biology because it is the most
versatile atom on Earth. Because of its four valence electrons,
it can form many covalent bonds. With different
combinations of single and double bonds, an almost limitless
array of molecular shapes is possible.

The formation of carboncarbon bonds was an important

event in chemical evolution.

Functional Groups: Determinants of Chemical Behaviour

The carbon atoms in an organic molecule furnish the skeleton

that gives the molecule its overall shape.

Amino and carboxyl groups: Attract or drop a proton, respectively
Carbonyl groups: Sites of reactions that link molecules into larger, more-

complex compounds
Hydroxyl groups: Act as weak acids
Phosphate groups: Have two negative charges
Sulfhydryl groups: Link together via disulfide bonds

Canadian Research 2.1 The Carbon-Rich Tagish Lake Meteorite

Most asteroids land in oceans and unpopulated regions and are

never found, but in January 2000 a meteorite landed near Atlin,

BC.
Fortunately when fragments were collected they were handled
with gloves and were quickly frozen.
This meteorite was unusual because:
It contained carbonaceous chondrites that date from the birth of our solar

system.
It contained a lot of organic molecules, including amino acids.

Canadian Research 2.1 The Carbon-Rich Tagish Lake Meteorite

Carbon like most other atoms is created within older stars by thermonuclear

reactions fusing helium nuclei together.

The meteorite was analyzed by Peter Brown from the University

of Western Ontario and others.

They found the asteroid contained:
3.7% carbonate minerals such as FeCO 3 and
1.7% other types of carbon-containing molecules.

Because the overall carbon content of this meteorite is

unexpectedly high, this meteorite may be very old. The Tagish

Lake meteorite may be the most primitive object ever studied in a
laboratory.

Ch 2 Summary
You should be able to
Determine which molecule would be more stable in your blood: one with
an ionic bond or one with a covalent bond.
Describe why water is such an excellent solvent.
Describe why buffers are important
Determine which chemical reactions would tend to be spontaneous or not
Describe the process of chemical evolution
Draw the different functional groups
Predict how a molecule with a functional group might behave

Ch 3: Key Concepts
Most cell functions depend on proteins.
Amino acids are the building blocks of proteins. Amino acids
vary in structure and function because their side chains vary
in composition.
Proteins vary widely in structure. The structure of a protein
can be analyzed at four levels that form a hierarchythe
amino acid sequence, substructures called -helices and pleated sheets, interactions between amino acids that dictate a
proteins overall shape, and combinations of individual
proteins that make up larger, multiunit molecules.
In cells, most proteins are enzymes that function as catalysts.
Chemical reactions occur much faster when they are
catalyzed by enzymes. During enzyme catalysis, the reactants
bind to an enzymes active site in a way that allows the
reaction to proceed efficiently.

Revisiting the Theory of Chemical Evolution

Modern life arose through a series of endergonic chemical
reactions.
1. Production of small organic compounds
i.e., formaldehyde (H2CO), hydrogen cyanide (HCN)

Formation of mid-sized molecules from these small compounds

i.e., amino acids, simple sugars
These molecules combined with ocean water to form
prebiotic soup.
3. Mid-sized building blocks combine to form large molecules.
i.e., proteins, complex carbohydrates
4. Life became possible when one of these large molecules selfreplicated.
2.

Early Origin-of-Life Experiments

Could the first steps of chemical evolution have occurred on
ancient Earth?
To find out, Stanley Miller combined methane (CH4), ammonia

(NH3), and hydrogen (H2) in a closed system with water, and

applied heat and electricity as an energy source.
The products included hydrogen cyanide (HCN) and
formaldehyde (H2CO), important precursors for more-complex
organic molecules and amino acids.
In more recent experiments, amino acids and other organic
molecules have been found to form easily under these
conditions.

The Structure of Amino Acids

All proteins are made from just 20 amino acid building
blocks.

All amino acids have a central carbon atom that bonds to NH2,
COOH, H, and a variable side chain (R-group).

In water (pH 7), the amino and carboxyl groups ionize to

NH3+ and COO, respectivelythis helps amino acids stay in
solution and makes them more reactive.

The Nature of Side Chains

The 20 amino acids differ only in the unique R-group attached
to the central carbon. The properties of amino acids vary
because their R-groups vary.

Functional Groups Affect Reactivity

R-groups differ in their size, shape, reactivity, and interactions

with water.
1.
2.

Nonpolar R-groups: hydrophobic; do not form hydrogen bonds;

coalesce in water
Polar R-groups: hydrophilic; form hydrogen bonds; readily dissolve
in water

Amino acids with hydroxyl, amino, carboxyl, or sulfhydryl

functional groups in their side chains are more chemically

reactive than those with side chains composed of only carbon
and hydrogen atoms.

Monomers and Polymers

Many mid-size molecules, such as amino acids and nucleotides,

are individual units called monomers. They link together

(polymerize) to form polymers, such as proteins and nucleic
acids.

Macromolecules are very large polymers made up of many

monomers linked together.

Thus, proteins are macromolecules consisting of linked amino

acid monomers.

Assembling and Breaking Apart Polymers

Polymerization requires energy and is nonspontaneous.
Monomers polymerize through condensation (dehydration)

reactions, which release a water molecule.

Hydrolysis is the reverse reaction, which breaks polymers apart

by adding a water molecule.

In the prebiotic soup, hydrolysis is energetically favourable

and thus would predominate over condensation. However,

polymers clinging to a mineral surface are protected from
hydrolysis, and thus polymerization of the amino acids into
proteins may have occurred spontaneously.

The Peptide Bond

Condensation reactions bond the carboxyl group of one amino

acid to the amino group of another to form a peptide bond.

A chain of amino acids linked by peptide bonds is called a

polypeptide.
Polypeptides containing fewer than 50 amino acids are called

oligopeptides (peptides).
Polypeptides containing more than 50 amino acids are called proteins.

Polypeptide Characteristics
Within the polypeptide, the peptide bonds form a backbone

with three key characteristics:

1.

R-group orientation

2.

Directionality

3.

Side chains can interact with each other or water.

Free amino group, on the left, is called the N-terminus.
Free carboxyl group, on the right, is called the C-terminus.

Flexibility

Single bonds on either side of the peptide bond can rotate, making the
entire structure flexible.

What Do Proteins Do?

Proteins are crucial to most tasks required for cells to exist:
Catalysis enzymes speed up chemical reactions.
Defence antibodies and complement proteins attack pathogens.
Movement motor and contractile proteins move the cell or molecules

within the cell.

Signalling proteins convey signals between cells.
Structure structural proteins define cell shape and comprise body
structures.
Transport transport proteins carry materials; membrane proteins
control molecular movement into and out of the cell.

Canadian Research 3.1 Designing New Proteins

Scientists use proteins as tools in experiments, such as
the green fluorescent protein from jellyfish which is
used to make different parts of a cell visible.
Some scientists are now designing their own proteins.
Researchers, Brian Bryksa, Yasumi Horimoto, and
Rickey Yada, from the University of Guelph have
created a new protein from a combination of a cow
protein that kills harmful bacteria and a pig enzyme that
works in the stomach and cuts up other proteins.

Canadian Research 3.1 Designing New Proteins

The new protein is designed to travel to the location of a
bacterial infection
- the enzyme portion will cut the hybrid protein in two
- this releases the antimicrobial portion to fight the
bacteria
This protein may be used in human or agriculturally
important plants or animals.

What Do Proteins Look Like?

Proteins can serve diverse functions in cells because they are
diverse in size and shape as well as in the chemical properties
of their amino acids.

All proteins have just four basic levels of structure: primary,

secondary, tertiary, and quaternary.

Primary Structure
A proteins primary structure is its unique sequence of amino

acids.
Because the amino acid R-groups affect a polypeptides

properties and function, just a single amino acid change can

radically alter protein function.

Secondary Structure
Hydrogen bonds between the carbonyl group of one amino

acid and the amino group of another form a proteins secondary

structure.
A polypeptide must bend to allow this hydrogen bonding, forming:

-helices
-pleated sheets

Secondary structure depends on the primary structure.

Some amino acids are more likely to be involved in

-pleated sheets.

-helices; others, in

The large number of hydrogen bonds in a proteins secondary

structure increases its stability.

Canadian Research 3.2 Spider Silk Proteins

Spiders produce several types of silk, one type is dragline silk,

which a spider uses in case it falls. This silk is six times

stronger than a steel fibre of the same diameter.
Its strength is due to the structure of its proteins. They comprise

mostly -pleated sheets, and it is the sum total of all the

backbone-to-backbone hydrogen bonds that gives the material
its strength.
Efforts are under way to mass-produce spider-silk proteins for

use as surgical sutures, bullet proof vests, and other applications

requiring a strong yet lightweight material.

Canadian Research 3.2 Spider Silk Proteins

Spiders anchor
themselves and use
dragline silk as a safety
line.
Is the dragline silk
strong enough to stop a
spider from falling?
Scenario 1 - dragline
failed >50%
Scenario 2 - dragline
failed 90%

Canadian Research 3.2 Spider Silk Proteins

When researchers tested the strength of the silk, they found that

it wouldnt be able to stop a spider from falling.

However, draglines rarely break when spiders fall - why?
Spiders have a couple of tricks:
As they fall they continue to release new silk
Within their spinnerets, they have internal friction brakes and as they
produce their new silk, they put on their brakes.

Tertiary Structure
The tertiary structure of a polypeptide results from

interactions between R-groups or between R-groups and the

peptide backbone.
These contacts cause the backbone to bend and fold, and contribute to the

distinctive three-dimensional shape of the polypeptide.

R-group interactions include hydrogen bonds, hydrophobic

interactions, van der Waals interactions, covalent disulfide

bonds, and ionic bonds.

R-group Interactions That Form Tertiary Structures

Hydrogen bonds form between hydrogen atoms and the

carbonyl group in the peptide-bonded backbone, and between

hydrogen and negatively charged atoms in side chains.
Hydrophobic interactions within a protein increase stability of

surrounding water molecules by increasing hydrogen bonding.

R-group Interactions That Form Tertiary Structures

van der Waals interactions are weak electrical interactions

between hydrophobic side chains.

Covalent disulfide bonds form between sulphur-containing R-

groups.
Ionic bonds form between groups that have full and opposing

charges.

Quaternary Structure
Many proteins contain several distinct polypeptide subunits that

interact to form a single structure.

The bonding of two or more subunits produces quaternary

structure.

Summary of Protein Structure

Note that protein structure is hierarchical.
Quaternary structure is based on tertiary structure, which is based in
part on secondary structure.
All three of the higher-level structures are based on primary structure.
The combined effects of primary, secondary, tertiary, and

sometimes quaternary structure allow for amazing diversity in

protein form and function.

Folding and Function

Protein folding is often spontaneous, because the hydrogen

bonds and van der Waals interactions make the folded molecule
more energetically stable than the unfolded molecule.
A denatured (unfolded) protein is unable to function normally.
Proteins called molecular chaperones help proteins fold

correctly in cells.

Prions and Protein Folding

Prions are improperly folded forms of normal proteins that are

present in healthy individuals.

Amino acid sequence does not differ from a normal protein, but shape is

radically different.

Prions can induce normal protein molecules to change their

shape to the altered form.

An Introduction to Catalysis
Catalysis may be the most fundamental of protein functions.
Reactions take place when:
Reactants collide in precise orientation
Reactants have enough kinetic energy to overcome repulsion between the
electrons that come in contact during bond formation

An Introduction to Catalysis

Enzymes perform two functions:

1. Bring substrates together in precise orientation so that the electrons

involved in the reaction can interact

2. Decrease the amount of kinetic energy reactants must have for the
reaction to proceed

Activation Energy and Rates of Chemical Reactions

The activation energy (Ea) of a reaction is the amount of free

energy required to reach the intermediate condition, or

transition state.
Reactions occur when reactants have enough kinetic energy to

reach the transition state.

The kinetic energy of molecules is a function of their temperature.

Thus, reaction rates depend on:

The kinetic energy of the reactants
The activation energy of the particular reaction (the free energy of the
transition state)

Catalysts and Free Energy

A catalyst is a substance that lowers the activation energy of a

reaction and increases the rate of the reaction.

Catalysts lower the activation energy of a reaction by lowering

the free energy of the transition state.

Catalysts do not change G and are not consumed in the

reaction.

Enzymes
Enzymes are protein catalysts and typically catalyze only one

reaction.

Most biological chemical reactions occur at meaningful rates

only in the presence of an enzyme.

Enzymes:
1.
2.

Bring reactants together in precise orientations

Stabilize transition states

Protein catalysts are important because they speed up the

chemical reactions that are required for life.

How Do Enzymes Work?

Enzymes bring substrates together in specific positions that

facilitate reactions, and are very specific in which reactions they

catalyze.

Substrates bind to the enzymes active site.

Many enzymes undergo a conformational change when the

substrates are bound to the active site; this change is called an

induced fit.

Interactions between the enzyme and the substrate stabilize the

transition state and lower the activation energy required for the
reaction to proceed.

The Steps of Enzyme Catalysis

Enzyme catalysis has three steps:
1. Initiation

2.

Transition state facilitation

3.

Substrates are precisely oriented as they bind to the active site.

Interactions between the substrate and active site R-groups lower the
activation energy.

Termination

Reaction products are released from the enzyme.

Figure 3.21 Enzyme Action C an Be Analyzed as a Three-Step Process.

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Do Enzymes Act Alone?

Some enzymes require cofactors to function normally. These

are either metal ions or small organic molecules called

coenzymes.
Most enzymes are regulated by molecules that are not part of

the enzyme itself.

Enzyme Regulation
Competitive inhibition occurs when a molecule similar in size

and shape to the substrate competes with the substrate for

access to the active site.
Allosteric regulation occurs when a molecule causes a change

in enzyme shape by binding to the enzyme at a location other

than the active site.
Allosteric regulation can activate or deactivate the enzyme.

What Limits the Rate of Catalysis?

Enzymes are saturable; in other words, the rate of a reaction is

limited by the amounts of substrate present and available

enzyme.
The speed of an enzyme-catalyzed reaction increases
linearly at low substrate concentrations.
The increase slows as substrate concentration increases
The reaction rate reaches maximum speed at high substrate
concentrations.
All enzymes show this type of saturation kinetics.

At some point, active sites cannot accept substrates any

faster, no matter how large the concentration of substrates

gets.

Physical Conditions Affect Enzyme Function

Enzymes function best at some particular temperature and pH.
Temperature affects the movement of the substrates and enzyme.
pH affects the enzymes shape and reactivity.

Rate of Enzyme-Catalyzed Reactions

To summarize, the rate of an enzyme-catalyzed

reaction depends on:

1. Substrate concentration
2. The enzymes intrinsic affinity for the substrate
3. Temperature
4. pH

Was the First Living Entity a Protein?

Several observations argue that the first self-replicating

molecule on Earth was a protein:

1.
2.
3.

Amino acids were abundant in the prebiotic soup.

Proteins are the most efficient catalysts known.
A self-replicating molecule had to act as a catalyst for the assembly
and polymerization of its copy.

However, the first self-replicator probably needed to have a

mold or a templatesomething not found in proteins.

Summary
You should be able to
Draw an amino acid and indicate the variable R group
Predict how a protein is composed of mostly acidic and polar R groups
would interact with water.
Describe how the four levels of protein structure affect the shape and
function of a protein.
Describe the major functions of proteins in a cell.
Describe how enzymes are regulated.
Predict how a change in pH will affect an enzyme.
Predict what would happen to a cell if one enzyme in a crucial pathway
was not correctly regulated.

Chapter 2

2014 Pearson Canada, Inc.

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