Non-lab content
1. Charges of subatomic particles
Proton – positive; neutron – neutral; electron – negative
2. The three categories of elements
Metals, nonmetals, and metalloids
3. The atomic number is the . . .
The number of protons or electrons
4. The atomic mass is the . . .
The weighted average of the protons and neutrons of all of an element’s
isotopes
5. Two pieces of information a chemical formula gives are . . .
a. The elements in the compound
b. The ratio of the elements
6. Similarities and differences between ionic, covalent, and H bonds and
van der Waals forces
Ionic – electrons are transferred; forms ions
Covalent – electrons are shared; forms single, double, and triple bonds;
stronger and far more common in organisms than ionic
H bonds – covalent bond between H and O or N; found commonly
between H2O molecules
Van der Waals – forces that form between adjacent molecules;
attractions between oppositely charged regions of molecules
-- All three involve interactions between electrons (transferred, shared,
or attracted)
7. Why water is polar and explain the cause of this polarity
a. It’s polar because there is an uneven distribution of electrons between
the O and H atoms
b. The O atom has 8 protons in its nucleus; therefore it attracts H
electrons closer to it, making it slightly negative and the H atoms slightly
positive.
8. Cohesion and adhesion
Cohesion – the attraction between molecules of the same substance
Example – hydrogen bonding between the water molecules
Adhesion – the attraction between molecules of different substances
Example – capillary action in plants (Water is attracted to the xylem
(root) tissue.)
9. Solution, solvent, and solute
Solution –even mixture of a solvent and a solute
Solvent – a substance that dissolves a solute
Solute – a substance that is dissolved by a solvent
10.
pH scale, acids, bases, and buffers
pH scale – measurement system used to measure the concentration of
hydrogen ions (H+) in a solution; ranges from 0 to 14 (0=most acidic;
14=most basic)
Acids – compounds that form hydrogen ions (H+) in solution
Bases – compounds that form hydroxide ions (OH-) in solution
Buffers – weak acids or bases that can react with strong acids or bases
to help prevent sharp, sudden changes in pH (a.k.a. Tums, Rolaids)
11.
Organic chemistry is . . .
the study of compounds that contain carbon
12.
Explain why carbon is such a unique and versatile atom.
a. It has four valence electrons, allowing it to bond with many other
elements.
b. C atoms can easily bond with other C atoms, forming long chains
rings, or fullerenes (Buckeyballs).
13. Know what a monomer and a polymer are, and be able to give
examples.
Monomer – smaller units of a macromolecule; they make up polymers
Polymer – larger units of a macromolecule
Examples – amino acids make up proteins; sugars make up carbs;
nucleotides make up nucleic acids
14.
What are the four “biomolecules?”
“PNCL Park” – proteins, nucleic acids, carbohydrates, lipids
15. The three elements that make up carbs and their ratio; functions of
carbs; suffix of carbs (sugars); monomer of carbs
Three elements – CHO
Ratio – 1:2:1
Functions – a. main source of energy for organisms
b. used to make cellular support structures (plant cell wall)
Suffix – “-ose”
Monomer - monosaccharides
16. Three main groups of lipids; functions of lipids; monomers and three
elements that make a lipid
Three groups – fats, oils, and waxes
Functions – a. energy storage in organisms
b. necessary part of cell membranes
Monomers – glycerol and fatty acid
Elements - CHO
17.
Definitions of saturated and unsaturated fats
Saturated – the lipid has the maximum # of H atoms in it; it is saturated
with hydrogen; all single bonds; animal fats; usually solid at room temp.;
unhealthy 
Unsaturated – the lipid does not have the maximum # of H atoms; it is
unsaturated with hydrogen; has at least one C=C bond; plant fats;
usually liquid at room temp.; healthier 
18. Elements in a nucleic acid; monomer of nucleic acids; function of
nucleic acids
Elements – PONCH
Monomer – nucleotide
Function – store and transmit genetic information
RNA and DNA are the two nucleic acids.
19. Elements that make up proteins; monomer of proteins; how amino
acids are different from one another; functions of proteins; suffix of
proteins
Elements – CHONS
Monomer – amino acid
Amino acid difference – the R- group
Some Functions – a. control rates of reactions
b. form bones and muscles
c. transport substances into/out of cells
d. help fight disease (antibodies)
Suffix – “-ine”
20a. Activation energy is . . .
the energy needed to start a chemical reaction
20b. Main function of all enzymes; suffix of most enzymes
Function – they significantly lower the activation energy needed to start
a chem rxn
Suffix – “-ase”
20c. A substrate is . . .
The molecule that reacts with an enzyme; the molecule that the enzyme
catalyzes (breaks down)
20d. An active site is . . .
The area on the enzyme to which the substrate binds; this is where the
substrate is catalyzed
20e. How can a substrate and active site be compared to a lock and key?
The active site and its substrate have complementary shapes, like a lock
and key; the active site is the lock and the substrate is the key
20f. Explain the induced-fit model. Why is it a better model than the lockand-key model?
The theory or model that currently best describes the complementary
nature of enzymes and their substrates is the “induced-fit” model. This
model basically states that as the active site and substrate come into close
proximity, their structures slightly modify in order to achieve the best
possible fit. The induced fit model replaced the incorrect “lock-and-key”
model which did not account for the subtle structural changes necessary for
the chem rxns to occur.
20g. Explain how an enzyme can become denatured.
If an enzyme is subjected to high/low temperatures, high/low pH,
pressure, or some non-competitive inhibitors (like poisons), its 3-D
shape will change (denature), rendering it non-functional.
20h. Give two reasons why enzymes are specific to their substrates.
a. The shapes of the enzyme and its substrate are complementary.
b. The enzyme has the opposite charge of its substrate.
20i. Explain competitive and non-competitive inhibition. Which is worse
and why?
In some cases there are molecules that are similar in size and shape
to the true substrate molecule. These “imposter” molecules called
competitive inhibitors may fit into the enzyme’s active site even though
the enzyme cannot react with them. Although the “inhibitor” occupies the
active site for only a brief period, while there it prevents the true substrate
molecule from entering, thus s l o w i n g the catalytic activity of the
enzyme.
Non-Competitive Inhibition can result when substances combine with the
enzyme to form compounds in the active site or change the electrical
charge of the active site. This results in the total loss of catalytic activity
and is a dangerous situation. Many poisons such as cyanide and certain
heavy metal ions such as silver, lead and mercury are non-competitive
inhibitors to many enzymes.
20j. Many organic co-enzymes can be classified as vitamins. What is their
function?
Co-Enzymes are best represented by vitamins that help enzyme
function by binding to specific substrates. The substrates are then directed
to the proper enzyme so that the substrate concentration at the active site
is increased leading to better enzyme performance. Vitamins are like
substrate “shepherds,” herding the substrates to the enzymes.
What to know from the labs/activities
Liver Lab
a. What was the purpose of observing the effects of MnO2?
To compare the effects of an inorganic catalyst (MnO2) with an
organic one (catalase).
b. Is MnO2 a catalyst? Is MnO2 an enzyme? Why or why not?
It is not an enzyme (because it’s inorganic), but it is a catalyst
because it brought about a chemical rxn.
c. What effect did fractionating cells (grinding in the mortar) have on the
catalytic activity of catalase? Why?
Fractionation increased the catalytic activity because it opened the
cells, thereby releasing more catalase enabling it to catalyze H2O2 at
a much faster rate.
d. What effect did boiling and HCl have on the catalytic activity of
catalase?
Boiling and HCl eliminated the catalytic activity because it denatured
the enzymes. (boiling due to high temp; HCl due to low pH)
e. How do you think the reaction would be altered if the concentration of
peroxide used was greater than the 3% we used? Explain.
The rxn would increase because the concentration of the substrate
would be greater.
f. What is the purpose of performing the splint test? What does a
positive result indicate to you about the catalytic activity of the
enzyme?
The splint test determined if a flammable gas was produced (in this
case, oxygen). The reignition of the splint indicates that the catalase
was functioning, i.e., breaking down H2O2 into O2 and H2O.
g. In what type of cell is catalase abundantly found?
Red blood cells
h. What was the purpose of observing the sand in H2O2?
To prove that the sand had no effect in causing the increased
catalytic activity in the
bloody pulp test.
Organic Compounds Indicator Lab
1. Know which indicator is used to identify which organic compound. Also
know the positive and negative colors. Memorize the following table.
Indicator
Organic
Compound
Lugol’s iodine
Polysaccharides
(starch)
Benedict’s solution Mono-,
disaccharides
Sudan IV
Lipids
Coagulation
Proteins
Biuret
Giemsa
Indophenol
Amino acids
Nucleic acids
Vitamin C
Positive Result
Negative Result
Blue-black
Amber
Orange
Sky blue
Crimson/scarlet
Heat causes
coagulation
Purple/violet
Minty-mossy green
Clear
Maroon
No coagulation
Very light blue
Royal blue
Royal blue
Hydrocarbon Structure Activity
1. Number of electrons needed for a stable carbon atom
8
2. Explain what a hydrocarbon is.
It’s the simplest organic compound made of only C and H. Many of them
are combustible.
3. The three suffixes of hydrocarbons and what they mean
-ane = single bond
-ene = double bond
-yne = triple bond
4. Be able to identify pictures of hydrocarbons
The chemical formulas are:
methane (CH4)
ethane (C2H6)
ethene (C2H4)
ethyne (C2H2)
propane (C3H8)
propene (C3H6) propyne (C3H4)
butane (C4H10 – straight chain)
isobutane (C4H10 – branched chain)
Toothpickase Activity
1. Know the answers to the three questions that accompanied the activity.
Substrate – toothpicks
Competitive inhibitors – pins
Active site – your fingertips
Product – broken toothpicks
It was called “toothpickase” because the suffix “-ase” is used as a suffix
for enzymes. Also, enzymes are usually named after their substrates (in
this case, toothpicks).
Crossed fingers represented a denatured enzyme because their shape
changed, like a denatured enzyme.
Amylase Lab, a.k.a. “Cracker Spit Lab”
Conclusion Questions
Part I
1. What color is Lugol’s iodine normally?
Amber
2. Explain what was happening to the iodine (at the molecular level)
after it was added to the potato slice.
The iodine entered the potato cells as its natural amber color.
Eventually it came into contact with the starch molecules in the
leucoplasts and turned black. The iodine “slid” into the helical
structure of amylose and amylopectin and reflected bluish-black.
Part II
3. What was the color of the iodine after you added it to the sugar?
WHY?
Amber, because there is no starch in sugar
4. What was the color of the iodine after you added it to the crushed
crackers? WHY?
Black, because crackers contain starch
5. What was the purpose of the sugar and crushed cracker?
The sugar was the negative control (no color change; received no
amylase) and the cracker was the positive control (color change;
received no amylase). BTW, amylase was the manipulated variable.
6. Why did one partner chew for one minute and the other chew for
four?
So that we could see the difference between the digestion of the
cracker after one minute and the digestion after four minutes. The
iodine was a darker color after one minute because the starches had
not been broken down as much as after four minutes by the amylase.
7. Why did you and your partner spit the cracker out at the same time?
So that there wasn’t one cracker mush being digested in the Petri
dish while the other one was still being chewed.
8. Explain what was happening in the iodine (at the molecular level)
after it was added to the cracker mush.
Same thing as what was happening in the potato
9. Why did you get different results between the cracker mushes?
The one minute cracker contained more starches because it had not
been exposed to the amylase as long as the four minute cracker
10. Is this investigation qualitative or quantitative? Explain your answer.
It’s qualitative because the results were observed (color changes)
and no numerical data were collected.