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How Matter is Organized

Chemistry is the science of the


structure and interactions of
matter.
all living things consist of matter.

Matter is anything that


occupies space.
mass is the amount of matter in
any object.
weight is the force of gravity
acting on matter
Does air have matter?

Chemical Elements
Elements are substances that can not be split
into simpler substances by ordinary means.
112 elements ( 92 occur naturally )
26 of naturally occurring elements are in the body
represented by chemical symbols ( first 1-2 letters
of name )

4 elements form 96 % of the bodys mass


hydrogen, oxygen, carbon and nitrogen

Trace elements are present in tiny amounts


such as copper, tin, selenium & zinc

Structure of Atoms
Atoms are the smallest units of
matter that retain the
properties of an element
Atoms consist of 3 types of
subatomic particles
protons, neutrons and
electrons
Nucleus contains protons (p+) &
neutrons (neutral charge)
Electrons (e-) surround the
nucleus as a cloud (electron
shells are designated regions of
the cloud)

Atomic Number & Mass Number

Atomic number is number of protons in the nucleus. .


Mass number is the sum of its protons and neutrons.

Isotopes

Molecule, Element, compound


Molecule= more than one atom existing in union
Element= Molecule contains identical atoms
Compound: Molecule contains different atoms

IONS: Charged particles


When an atom gains or loses electrons ions are
formed
Positively charged= cation
Negatively charged = anion

Free Radicals

Atom with an unpaired electron in its outmost


shell
Unstable and highly reactive
Can become stable
by giving up electron
taking one off another molecule (breaking apart
important body molecules)

Free Radicals & Your Health

Produced in your body by absorption of energy in ultraviolet


light in sunlight, x-rays, by breakdown of harmful
substances, & during normal metabolic reactions
Linked to many diseases -- cancer, diabetes, Alzheimer,
atherosclerosis and arthritis
Damage may be slowed with antioxidants such as vitamins C
and E, selenium & beta-carotene (precursor to vitamin A)

Chemical Bonds
Bonds hold together the
atoms in molecules and
compounds
An atom with a full outer
electron shell is stable and
unlikely to form a bond with
another atom
Octet rule states that
biologically important
elements interact to
produce chemically stable
arrangements of 8
electrons in the valence
shell.
Whether electrons are
shared, donated or acquired
determines the types of
bonds formed

Covalent Bonds

Atoms share electrons


to form covalent bonds
Electrons spend most of
the time between the 2
atomic nuclei

single bond = share 1pair


double bond = share 2 pair
triple bond = share 3 pair

Polar Covalent Bonds


Unequal sharing of electrons between atoms.
In a water molecule, oxygen attracts the
hydrogen electrons more strongly
Oxygen has greater electronegativity as
indicated by the negative Greek delta sign.

Ionic Bonds
Positively and negatively
charged ions attract each
other to form an ionic bond
In the body, ionic bonds
are found mainly in teeth
and bones
An ionic compound that
dissociates in water into +
and - ions is called an
electrolyte

The Ionic Bond in Sodium Chloride


Sodium loses an electron
to become Na+ (cation)
Chlorine gains an electron
to become Cl- (anion)
Na+ and Cl- are attracted
to each other to form the
compound sodium chloride
(NaCl) -- table salt
Ionic compounds generally
exist as solids

Hydrogen bonds

Hydrogen bonds are the most important inter


molecular force of attraction .
Formed by the attraction between slightly positive
Hydrogen atom and a slightly negative atom of
another element.
Too weak to create molecules but creates shapes
and stabilizes large molecules like proteins or
nucleic acids

Chemical Reactions
When new bonds form or old bonds are broken
Metabolism is all the chemical reactions in the body

Energy and Chemical Reactions


Chemical reactions involve energy changes
Law of conservation of energy
energy can neither be created nor destroyed--just
converted from one form to another

Reactions that yield energy = Exergonic reactions


(Larger to smaller molecules)
AB A + B
Reactions that require energy to occur= Endergonic
reactions (smaller to larger molecules )
A + B AB

Energy Transfer in Chemical


Reactions
Chemical reactions usually involve
both
Human metabolism couples
exergonic and endergonic
reactions, so that the energy
released from one reaction will
drive the other.
Glucose breakdown releases energy
used to build ATP molecules that
store that energy for later use in
other reactions

Activation Energy
Atoms, ions & molecules
are continuously moving
& colliding
Activation energy is the
collision energy needed
to break bonds & begin a
reaction
Increases in concentration & temperature, increase the
probability of 2 particles colliding
more particles in a given space as concentration is raised
particles move more rapidly when temperature is raised

Catalysts/Enzymes
Normal body temperatures
and concentrations are too
low to cause chemical
reactions to occur
Catalysts speed up chemical
reactions by lowering the
activation energy needed to
get it started
Catalysts orient the
colliding particles properly
so that they touch at the
spots that make the
reaction happen
Catalyst molecules are
unchanged and can be used
repeatedly to speed up
similar reactions.

Free Energy and


Activation
Energy Tutorial

Synthesis Reactions-Anabolism
Two or more atoms, ions or
molecules combine to form
new & larger molecules
All the synthesis reactions
in the body together are
called anabolism
Usually are endergonic
because they absorb more
energy than they release
Example
combining amino acids to
form a protein molecule

Decomposition Reactions-Catabolism
Large molecules are split into
smaller atoms, ions or
molecules
All decomposition reactions
occurring together in the body
are known as catabolism
Usually are exergonic since
they release more energy than
they absorb

Inorganic Compounds & Solvents


Most of the chemicals in the body are
compounds
Inorganic compounds

usually lack carbon & are structurally simple


water, salts, acids and bases

Organic compounds

contain carbon & usually hydrogen


always have covalent bonds

Dissociation

pH - measure or acidity/alkalinity pH = - log [H+]


acidic < 7 < basic
Acids-raise H+ content
Bases-lower H+ content:
release OH- or accepts H+

1pH unit = 10x difference


1000 as many H+ in a pH of 5 as there are in 8
Buffer-takes up or releases H+ or OH- to prevent
changes in pH. In the bicarbonate system, H2CO3 H+
base acceptor, HCO3- acid acceptor
What happens to shells in carbonated drinks?
Does Sea Ice Speed Up Ocean Acidification?
How does the bicarbonate system work in a blood plasma? In the ocean?

Ocean Acidification: 2, 3

Carbon dioxide
concentration in
metabolically active cells is
much greater than in
capillaries, so carbon
dioxide diffuses from the
cells into the capillaries.
About 7% of the CO2
directly dissolves in the
plasma. Another 23% binds
to the amino groups in
hemoglobin. The remaining
70% is transported in the
blood as bicarbonate ion.

Concept of pH
pH scale runs from 0 to
14 (concentration of H+
in soln.)
pH of 7 is neutral
(distilled water)
pH below 7 is acidic and
above 7 is alkaline

What is more acid than lemon?


In a test of pH levels, a glass of milk was found to have a pH of 6.0. A
glass of grape juice had a pH of 3.0. What is the relationship between
the pH levels of the milk and grape juice?
A The milk is 100 times more acidic than the grape juice
B The grape juice is 3 times more acidic than the milk
C The milk is 3 times more acidic than the grape juice
D The grape juice is 1000 times more acidic than the milk
How many more H+s do tomatoes have than bananas? Lemons than milk?
Bleach than soap?

Inorganic Acids, Bases & Salts


Acids, bases and salts always dissociate into ions
if they are dissolved in water
acids dissociate into H+
and one or more anions
bases dissociate into OHand one or more cations
salts dissociate into anions
and cations, none of which
are either H+ or OH-

Acid & bases react in the body to form salts


Electrolytes are important salts in the body that
carry electric current (in nerve or muscle)

Water & Its Properties

Most important inorganic compound in living


systems, Medium of nearly all chemical reactions
Polarity
uneven sharing of electrons
makes it an excellent solvent for ionic or polar substances
gives water molecules cohesion
allows water to moderate temperature changes

Participates as a product or reactant in certain


reactions in the body

hydrolysis reactions
water is added to a large molecule to separate it into
two smaller molecules
digestion of food
dehydration synthesis reaction
two small molecules are joined to form a larger
molecule releasing a water molecule

Water as a Solvent

Most versatile solvent known

polar covalent bonds (hydrophilic vs hydrophobic)


its shape allows each water molecule to interact
with neighboring ions/molecules

Water dissolves many substances

Water has a high surface tension


Water is wet
Water is attracted to itself, and this attraction,
due to H bonds is stronger than the attraction to
the air above
Adhesion and cohesion allow for capillary action
water transport in plants
Occurs as solid, liquid and gas within normal
temperature ranges on Earth

Water = good evaporative coolant


Heat of vaporization is also high

amount of heat needed to change from liquid to gas


evaporation of water from the skin removes large amount of
heat

B/c it takes a lot of energy to change water from a liquid to


a gas, it takes energy with it
Heat capacity is high
can absorb a large amount of heat with only a small increase in
its own temperature
large number of hydrogen bonds in water
bonds are broken as heat is absorbed instead of
increasing temperature of water
large amount of water in body helps lessen the impact of
environmental changes in temperature

Water as a Lubricant

Major component of lubricating fluids within the


body
mucus in respiratory and digestive systems
synovial fluid in joints
serous fluids in chest and abdominal cavities
organs slide past one another

Ice floats
Water has a high freezing point and lower density
as a solid than a liquid

Chemical Reactions
energy causes rearrangement of e-'s and new bonds, new
compounds are formed, E can be force of collision, heat,
electricity etc.
reactants yield product(s)
Balanced equations (energy cannot be created or
destroyed). Balance the following equations:
CH4 + O2 CO2 + H2O
CuO + NH3 Cu + H2O + N2
NH3 + O2 NO + H2O

CH4 + 2O2 = CO2 + 2H2O


3CuO + 2NH3 = 3Cu + 3H2O + N2
4NH3 + 5O2 = 4NO + 6H2O

Mixtures-- combination of substances in


which the individual components retain
their own properties

solutions-- or
more
substances
is
distributed evenly in another substance
solution=solvent(H2O)+solute(dissolvedparticles)

suspension-- particles of materials


temporarily mixed together (blood)
colloid-- particles larger than solution,
smaller than suspension (cytosol)

are

Chemistry Tutorial
The Biology Project:
http://www.biology.arizona.edu/biochemistry
/tutorials/chemistry/main.html

Carbon & Its Functional Groups

Properties of carbon atoms


forms bonds with other carbon atoms produce large,
stable molecules
with many different shapes (rings, straight or
branched chains)
Many functional groups can attach to carbon skeleton
esters, amino, carboxyl, phosphate groups (Table 2.5)
Very large molecules called macromolecules (polymers if all
monomer subunits are similar)

The properties of different biological molecules


depend on certain characteristic groupings of
atoms called functional groups.
If you know the properties of some of the
functional groups, you will be able to quickly look
at many simple biological molecules and get some
idea of their solubility and possible identity. The
names of the six most important functional groups
are:
Hydroxyl
Carbonyl
Carboxyl
Amino
Sulfhydryl
Phosphate

Hydroxyl
Two functional groups containing oxygen, the
hydroxyl and carbonyl groups, contribute to
water solubility.
Hydroxyl groups have one hydrogen paired
with one oxygen atom (symbolized as -OH).
Hydroxyl groups are not highly reactive, but
they readily form hydrogen bonds and
contribute to making molecules soluble in
water. Alcohols and sugars are "loaded" with
hydroxyl groups.

Genistein and daidzein, two phytoestrogens from legumes

Notice that the only difference between these two molecules


is the additional hydroxyl (-OH) group on genistein. Both
are typical isoflavones. Genistein, however, is considerably
more estrogenic than daidzein; chemists attribute this to
the influence of the additional hydroxyl group. The hydroxyl
groups are important for binding to estrogen receptors.

Carbonyl
Carbonyl groups have one oxygen atom doublebonded to a carbon atom (symbolized as -C=O).
Like hydroxyl groups, carbonyl groups contribute
to making molecules water-soluble. All sugar
molecules have one carbonyl group, in addition to
hydroxyl groups on the other carbon atoms.
Aldehyde groups, where the C=O group is at the end of
an organic molecule. A hydrogen atom is also located on
the same carbon atom.
Keto groups, where the C=O group is located within an
organic molecule. All sugars have either a keto or an
aldehyde group.

Carbonyl
-COH
C3H6O
aldehyde =
end (propanol)
ketone =
inside (acetone)

Carboxylic Acids

Carboxyl groups are weak acids, dissociating


partially to release hydrogen ions.The carboxyl
group (symbolized as COOH) has both a carbonyl
and a hydroxyl group attached to the same carbon
atom, resulting in new properties.
Carboxyl groups frequently ionize, releasing the H from the
hydroxyl group as a free proton (H+), with the remaining O
carrying a negative charge. Molecules containing carboxyl
groups are called carboxylic acids and dissociate partially
into H+ and COO.
Carboxyl groups are common in many biological molecules,
including amino acids and fatty acids.

Amino Group

Nitrogen in biological molecules usually occurs in


the form of basic amino groups.Nitrogen is
another abundant element in biological molecules.
Having a valence of 3, nitrogen normally forms
three covalent bonds, either single, double, or
triple bonds.
Amino groups (-NH2) are common functional groups
containing nitrogen. Amino groups are basic, and
often become ionized by the addition of a hydrogen
ion (H+), forming positively charged amino groups (NH3+).

Sulfhydryl

Sulfur is found mainly in proteins in the form of


sulfhydryl groups or disulfide groups.Like oxygen,
sulfur typically has a valence of 2, although it can
also have a valence of 6, as in sulfuric acid.
Sulfur is found in certain amino acids and proteins
in the form of sulfhydryl groups (symbolized as SH). Two sulfhydryl groups can interact to form a
disulfide group (symbolized as -S-S-).

Phosphate Groups
In biological molecules, phosphorus occurs mainly
in the form of acidic phosphate groups.
Phosphorus normally has a valence of 5. Its most
common functional group in organic molecules is as a
phosphate group (symbolized as OPO32-).
Phosphorus is covalently paired to 4 oxygen atoms
in phosphate groups: one P=O bond and three P-Obonds.

Importance of Functional Groups in


Biology

Function Groups Practice


Match the columns
1.
2.

3.
4.

5.
6.

Types of Organic compounds


Four major groups of organic
compounds, necessary for life are:
polymers
monomers____
Carbohydrates
monosacchrides
Lipids
fatty acids
Proteins
amino acids
Nucleic acids
nucleotides

Carbohydrates
Diverse group of substances from C, H, and O
ratio of one carbon atom for each water molecule
(carbohydrates means watered carbon)
glucose is 6 carbon atoms and 6 water molecules (H20)

Main function is to produce energy


3 sizes of carbohydrate molecules
monosaccharides
disaccharides
polysaccharides

Mono saccharides
one sugar

Called simple sugars


Contain 3 to 7 carbon atoms
(CH2O)n
We can absorb only 3 simple sugars
without further digestion in our small
intestine
glucose found in syrup or honey
fructose found in fruit
galactose found in dairy products

Disaccharides (two)
Formed by combining 2 monosaccharides by
dehydration synthesis (releases a water molecule)
Name of bond= Glycosidic bond
sucrose = glucose & fructose

Condensation Rxn & Dehydration


Synthesis
2 Condensation & Hydrolysis QT Mov

Disacchrides of distinction
glucose + fructose = sucrose
glucose + glucose = maltose
glucose + galactose = lactose

Polysaccharides
> 100s of monomers by
dehydration synthesis
In animals

Glycogen: glucose
polymer, found in liver &
skeletal muscle, when
blood sugar level drops,
liver hydrolyzes glycogen
to create and release
glucose into the blood

(many)

Polysaccharide

Lipids = fats, oils, steroids, waxes

Formed from C, H and O


18-25% of body weight
Hydrophobic
fewer polar bonds because of fewer oxygen atoms
insoluble in water
Combines with proteins for transport in blood
Lipoproteins
Three functional classes:
Storage lipid:
-Triglycerides: Common body fat.
Regulatory lipid:
- Steroids: act as hormone
- Eicosanoids: hormones
Structural lipid:
Phospholipids: Cell membrane
Glycolipids: Cell membrane

Triglycerides
Fats composed of a single glycerol molecule and 3
fatty acid molecules
three-carbon glycerol molecule is the backbone

Very concentrated form of energy


9 calories/gram compared to 4 for proteins &
carbohydrates
our bodies store triglycerides in fat cells if we eat
extra food

Triglyceride Formation
Triglycerides =
three fatty
acids attached
by dehydration
synthesis to
one molecule of
glycerol by an
ester bond
Figure 2.15

Saturation of Triglycerides

Determined by the
number of single or
double covalent bonds
in fatty acid
Saturated fats contain
single covalent bonds
and are covered with
hydrogen atoms----lard
Unsaturated are not
completely covered
with hydrogen---safflower oil, corn oil
Polyunsaturated fats
contain even less
hydrogen atoms----olive
and peanut oil

Regulatory lipids: Steroids


Formed from 4 rings of
carbon atoms joined
together
Common steroids
sex hormones, bile salts,
vitamins & cholesterol
Cholesterol found in animal
cell membranes
starting material for
synthesis of other
steroids
Which is most soluble in
water?

Eicosanoids
Lipid type derived from a fatty
acid called arachidonic acid
prostaglandins = wide variety of
functions

modify responses to hormones


contribute to inflammatory response
prevent stomach ulcers
dilate airways
regulate body temperature
influence formation of blood clots

leukotrienes = allergy &


inflammatory responses

Structural lipids
Phospholipids: Glycerol+ fatty acids + phosphate
Part of cell membrane. Ex. Lecithin.
Glycolipid: Glycerol+ fatty acid+ sugar chain.
Part of cell membrane surface.

Chemical Nature of Phospholipids


amphi pathic

head

tails

Lipid Behavior in Various


Environments
How do phospholipids behave
In an oil spill?
Submerged in water?
In a living cell?

Lipoproteins
What
determines
the density
of
lipoproteins?

Nucleic acids are chains of nucleotides


Three types: DNA, RNA, ATP
Function: Storage of genetic
information and energy
Nucleotides are composed of:
sugar, phosphate,nitrogenous base

Sugar = deoxyribose (DNA) or ribose (RNA & ATP)


DNA Bases = adenine, thymine, cytosine, guanine
RNA bases = adenine, uracil, cytosine, guanine
Base Pairing: A-T, G-C or A-U. Held together by
hydrogen bonds

DNA Structure
Huge molecules containing
C, H, O, N and phosphorus
Each gene of our genetic
material is a piece of DNA
that controls the synthesis
of a specific protein
A molecule of DNA is a
chain of nucleotides
Nucleotide = nitrogenous
base (A-G-T-C) + pentose
sugar + phosphate group

RNA Structure
Differs from DNA
single stranded
ribose sugar not
deoxyribose sugar
uracil nitrogenous base
replaces thymine
Types of RNA within the
cell, each with a specific
function
messenger RNA
ribosomal RNA
transfer RNA

Adenosine Triphosphate (ATP)

Temporary molecular storage of energy as it is


being transferred from exergonic catabolic
reactions to cellular activities

muscle contraction, transport of substances across cell


membranes, movement of structures within cells and
movement of organelles

Consists of 3 phosphate
groups attached to
adenine & 5-carbon
sugar (ribose)

Formation & Usage of ATP


Hydrolysis of ATP (removal of terminal phosphate
group by enzyme -- ATPase)
releases energy
leaves ADP (adenosine diphosphate)
Synthesis of ATP
enzyme ATP synthase catalyzes the addition of
the terminal phosphate group to ADP
energy from 1 glucose molecule is used during
aerobic respiration to create 36 to 38 molecules
of ATP

Amino Acid Structure


Central carbon atom
Amino group (NH2)
Carboxyl group (COOH)
Hydrogen
Side chains (R groups) vary between amino acids

Proteins
Contain carbon, hydrogen, oxygen, and
nitrogen
Constructed from combinations of 20
amino acids.
Levels of structural organization
primary, secondary and tertiary
shape of the protein influences its ability to form
bonds

Which Amino Acids


are hydrophobic?
How do you know?

Which Amino
Acids are
alkaline?
Why?

Formation of a peptide Bond

Dipeptides formed from 2 amino acids joined by a


covalent bond called a peptide bond
dehydration synthesis
Polypeptides chains formed from 10 to 2000 amino
acids.

Levels of Structural Organization

Primary is unique sequence of amino acids


Secondary is alpha helix or pleated sheet folding
Tertiary is 3-dimensional shape of polypeptide chain
Quaternary is relationship of multiple polypeptide chains

The four levels of protein


configuration

Primary is unique
sequence of amino acids
Secondary is alpha helix
or pleated sheet folding
Tertiary is 3-dimensional
shape of polypeptide
chain
Quaternary is
relationship of multiple
polypeptide chains

Protein Folding Tutorial:


Protein folding in Water

Bonds of protein Structure


Hydrogen bond forms
the secondary structure
Disulfide bonds stabilize
the tertiary structure of
protein molecules
Disulfide bond between
2 polypeptide chains
create quaternary
structure

Protein Denaturation
Function of a protein depends
on its ability to recognize and
bind to some other molecule
Hostile environments such as
heat, acid or salts will change
a proteins 3-D shape and
destroy its ability to function
raw egg white when cooked is
vastly different

Glycoprotein and Proteoglycan


Proteins exist in combination with sugar.
Glycoprotein: Protein + sugar chain. Found in cell
membrane. Serve as surface proteins.
Proteoglycan: Protein + sugar chain. Also present in
cell membrane. Can have enzymatic activity.

Enzymes
Enzymes are protein molecules that act as
catalysts by lowering Activation Energy
Enzyme = apoenzyme + cofactor
Apoenzymes are the protein portion
Cofactors are nonprotein portion

may be metal ion (iron, zinc, magnesium or calcium)


may be organic molecule derived from a vitamin

Enzymes usually end in suffix -ase and are named


for the types of chemical reactions they catalyze
How Enzymes Work
Enzyme Tutorial
Enzyme Catalysis

Enzyme Functionality
Highly specific

acts on only one


substrate

active site versus induced


fit

speed up only one


reaction

Very efficient

speed up reaction up to
10 billion times faster

Under nuclear control


Co-factors first bind to
the enzyme = enzyme
activated

Enzyme Structure Interactions


Lock and Key: shape and active
site of enz is only compatible
w/
substrate,
forming
substrate enzyme complex
-enz reused but are eventually
decomposed=constant synthesis
-usually end in "ase" and take
name of substrate

Factors Affecting Enzyme Action


Temperature:
40oC, denaturation
Enzyme Saturation
Concentration of substrate
pH
pepsin ( gastric protease) pH
2
trypsin (pancreatic protease)
pH 8

Saturation

Cofactors
Cofactors can aid how enzyme
works. If they are organic, then
they are coenzymes these are
enzyme activators
Allosteric
&
Cofactors
inhibitors
activators

Competitive

Pharmacological Enzyme
Inhibitors
Allosteric Regulation
Biochemical Pathway
Competitive vs Noncompetitive
Inhibitors

Competitive vs Noncompetitive Inhibitors

In this animation, the enzyme is olive, the substrate is green,


the competitive inhibitor is red and the products A & B are
yellow and blue. The enzyme has binding site into which either
the substrate or the competitive inhibitor may fit.
Which product, A or B, would most likely be a competitive
inhibitor?

The enzyme has 2 binding sites, one for the


substrate (the active site) and the other for the
allosteric activator (the regulatory site). Allosteric
Activation
Nerve gas permanently blocks pathways involved in nerve
message transmission, resulting in death.
Penicillin, the first of the "wonder drug" antibiotics,
permanently blocks the pathways certain bacteria use to
assemble their cell wall components.

Examples of Enzyme function


Ethylene levels cause changes in the production of different
enzymes, allowing fruits to ripen.
In eukaryotic cells the mRNA transcript undergoes a series
of enzyme regulated modifications.
The enzyme RNA-polymerase reads the DNA molecule in the
3' to 5' direction and synthesizes complementary mRNA
molecules that determine the order of amino acids in the
polypeptide.
ATP Synthase
DNA polymerase, ligase, RNA polymerase, helicase and

topoisomerase,

Positive Feedback
Amplification occurs when the stimulus is further
activated, which in turn initiates an additional
response that produces system change

Lactation in mammals
Onset of labor in childbirth
Ripening of fruit
Blood clotting

Estrogen & Progesterone in Female System

Negative Feedback/ Feedback


Inhibition
When the product is in abundance,
it binds competitively with its
enzyme's active site; as the
product is used up, inhibition is
reduced and more product can be
produced. In this way the
concentration of the product is
always controlled within a certain
range.

Operons in gene regulation


Temperature regulation in animals
Plants response to water
limitations

Resources

Animations:
Microbiology:
BioTopics Contents:
What is an Enzyme:
Lipid Behavior in Various Environments
Organic Molecules
Interactive Animations for Biochemical Processes
Biology Project Chemistry Tutorial
Chemistry Target Practice
Importance of Functional Groups
Functional groups Matching
Identify the Biomolecules Matching
"Hot Potatoes" Practice matching exercises
Factors that affect the rate of Chemical Reactions with Alka Seltzer
Properties of Water
Properties of Water & Transpiration
Enzyme Specificity Tutorial
Enzyme Kinetics Animation
Water Potential Quiz

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