The following informal questions will guide your studying
efforts towards the key conceptional ideas we have covered and
will strenghen your knowledge for the upcoming exam.
GOOD LUCK STUDYING AND PLEASE PHONE OR MAIL ME AS
QUESTIONS ARISE DURING YOUR REVIEW FOR THE EXAM!
For all exams:
NOTE: You should know specific vocabulary words and conventions we
have defined and not be afraid to use them!
YOU WILL BE REQUIRED TO PROVIDE DETAILED INFORMATION
AS WELL AS TO APPLY PRACTICAL LOGIC FROM
MAKE SURE YOU PREPARE YOURSELF FOR MULTIPLE TESTING
FORMATS AND STUDY YOUR MATERIAL KNOWING THAT THERE WILL
BE t/f, FILL IN THE BLANKS, SHORT ANSWER, AS WELL AS
MULTIPLE CHOICE. I WANT TO TEST YOU FOR YOUR KNOWLEDGE,
NOT YOUR ABILITY TO EXAMINE, THEREFORE THE FORMAT IS
DIVERSE AND UNBIASED.
First Exam Study Questions:
Omit the red questions for examination purposes
1. What are the 10 themes of the Study of Life? What is the hierachy of
organization from the atom to the community?
2. What is the smallest unit of life? of matter? What two men were
instrumental in developing the Cell Theory? How did they contribute?
3. What are the two major classes of cells? Name four characteristics
of ALL cells? Compare and contrast the prokaryotic from the eukaryotic
4. Who discovered DNA? What is a nucleotide? A genome? The double helix?
Complementary h-bonding? Know the structural differences between purines
5. What is the taxonomy of living organisms? How is it arranged? What
are the 3 domains? What are the 2 major theories upheld today and
established by Charles Darwin?
6. What are the two major forms of inquiry practiced by scientists
today? Be familiar with the scientific method and know the difference
between a theory and a hypothesis. How is science a social process?
7. Define the differences between matter, weight, mass, element, compound,
molecules, subatomic particles, atomic number, atomic weight, and mass number.
8. Which elements are life essential? Which comprise most of our body composition?
Which comprise only a few percentages? Which are termed trace elements?
Know the symbols, atomic weight, valence, and bonding capacity of these 25 of 92
9. What is a dalton? How much does a neutron weigh? If you know the weight and
charge of an element, can you calculate the number of protons, neutrons, or electrons
10. What's the difference between an isotope and an isomer?
11. How are radioactive isotopes harmful and useful in society?
12. What does potential energy have to do with electron shells or orbitals?
How is this information portrayed in the periodic table? What is the
difference between the number of unpaired electrons, valence, reactivity,
and inert chemicals?
13. What is this element? 1s2 2S2 Sp6 3S2 3p5 (HTML doesn't allow superscript!)
14. Describe the differences between ionic bonds, covalent bonds, and hydrogen
bonds. Give some good examples. What is the difference between a molecular
formula and a structural formula? Can a molecule have the same molecular
formula but a different structural formula? Would this make it a different
chemical, why or why not?
15. What is polarity? How can this be explained in terms of a dipole moment?
16. Why is water more structured than other liquids?
17. What are Van der Waals Interactions?
18. How does water provide stabilization of temperature? Define the difference
between heat and temperature? What is kinetic energy? Be able to perform calculations
with the units of temperature and heat. What is the heat of vaporization and the process
of evaporative cooling? What does H-bonding have to do with these processes?
19. How does water expand when it freezes, but other liquids do not? Why is this
20. Define solution, solvent, solutes, aqueous solution, hydrophillic, hydrophobic,
and Avogadro's number. Make up a solution 0.25 M glucose (add up all the atomic weights
from the structure you now know) - if our experiment only calls for one-half milliliter
of this molarity of glucose, how much will we need in g?
21. If MgSO4 has a FW of 120g and we add 60g into a Liter flask, how many molecules
will we have in our flask?
22. If our solution of MgSO4 has a hydroxide ion concentration of 0.01 what will
be the pH of the solution? What if the hydrogen concentration how changes by
1000 fold.....what will be the new pH of the solution?
23. What are some examples of weak acids and weak bases? What makes an acid or
base a strong one? What is a buffer? How does acid precipitation occur in our
environment and what damage can it encure?
24. Who were some of the early scientist that defined the field of organic
chemistry? What were some of their experiments? How does the definition
of organic chemistry differ from that of say the early 19th century?
25. Name 6 ways in which C atoms demonstrate versatility?
26. Given two structures, be able to identify whether the compounds are
structural, geometric, or enatiomer types of isomers. What is the
definition of a functional group? Know all 6 functional groups and
be able to build or take apart compounds if asked to add or subtract
a certain functional group. Know what type of compounds contain these
27. What is a monosaccharide? What are two classes of monosaccharides?
What type of reactions are used to build or disassemble disaccharides?
How do you make maltose, lactose, or sucrose?
28. What is a polysaccharide? Which of the following are used as
fuel - starch, cellulose, chitin, glycogen? What is a 1-4 linkage?
Where would you find 1-6 linkages? What is the difference between
alpha and beta glucose? Are microfibrils made out of which form?
29. Describe why fats, phospholipids, and steroids are hydrophobic?
How are triglycerides similar in structure to a phospholipid? What
are triglycerides used for biologically? Phospholipids (PLs)? Steroids?
30. Define saturated versus unsaturated fat? What is amphipathic?
What are two types of arrangements commonly found for PLs?
31. How do the four levels of proteins differ? What is the structure
of an amino acid, the building block of all proteins? Which amino
acids are classified into the following groups based upon side chain
(R)? - acidic, basic, nonpolar, polar? Which two functional groups
form a peptide bond? What is a glycosidic bond? What is a ester
32. What's the difference between the double helix and an alpha helix?
33. Define chaperone proteins, denaturation (and common causes), and
how scientists today discover protein structure?
34. Be able to model (draw) the Fluid Mosaic Model of the membrane
phospholipid bilayer and discuss properties such as its selective
permeability, its fluidity, its mosaicism, and its sidedness. How
was the model advanced from Gorter and Grendel to Davson and Danielli
to finally Singer and Nicolson?
35. What are six important functions (and give examples) of the PM?
Second Exam Study Questions:
1. Define metabolism. What is the difference between catabolic and
anabolic pathways? Why are these two types of pathways favorably coupled?
2. Define energy. What are the 3 types of energy important to
organisms? How are chemical reactions related to potential energy
and finally kinetic energy?
3. What are the first and second law of thermodynamics governing
4. Define free energy in vocabulary terms and in equation form. What
does it mean for a reaction to be spontaneous? Are enzymes required
for spontaneous reactions? If you want to have a reaction proceed,
how does a change in total enthalpy, temperature, entropy, or enzyme
affect the reaction?
5. Know the delta G values for respiration, hydrolysis of ATP,
photosynthesis, and a reaction at equilibrium.
6. Discuss what is meant by life being "Metabolic Disequilibrium".
7. What 3 types of work require the energy coupling by ATP? What is the
chemical structure of ATP (functional "groups")? What is the formula for
hydrolysis of ATP? How does ATP phosphorylate substrates and couple to
endergonic reactions? What is it called when a phosphate is removed
from a substrate?
8. What are 5 characteristics of the catalytic proteins, enzymes?
9. What are the 3 basic steps of ALL chemical reactions? Think about
this in terms of the energy profile. Be able to draw or interprete an
energy profile of a reaction. What part of the energy profile does an
enzyme modify? What part of the profile is unaffected by an enzyme?
10. What is the active site of an enzyme? How is this related to
the Induced Fit Model? How is this related to substrate specificity?
To saturation? What is the enzyme-substrate complex? How does the
active site promote the proper orientation of reactants?
11. How do you think temperature, pH, and co-factors influence the
12. Distinguish between competitive inhibition, noncompetitive inhibition,
and allosteric regulation? Is allosteric regulation inhibitory or excitatory?
Would you think that Feedback Inhibition acts at the active site? Why or why not?
What about Cooperativity?
13. Which substances are permeant across the PM? Which ones are highly
impermeant across the PM?
14. Specificity of transport of impermeant substances is determined by
the type of protein, but what determines the rate and direction of
how the substance will move?
15. What is simple diffusion? Does it require an input of energy?
16. How is passive transport different and similar to active transport?
17. If given an osmotic condition, be able to determine which way water
will flow across a semi-permeable membrane. If given a concentration
gradient, be able to determine which way a solute will flow. Understand
the terms isotonic, hypertonic, and hypotonic. Know how animal versus
plants cells would respond in each of the above external environments.
18. How does facilitated diffusion compare with simple diffusion?
19. Understand the cellular workings of the 3Na/2K ATPase pump. Understand
how the gradient built up through the expenditure of energy is created
by conformational changes induced by phosphorylation and dephosphorylation.
Why do all cells have an unequal distribution of charge? What is this
voltage difference called? What is an electrochemical gradient? When
do cells follow an electrochemical gradient...when at rest, or when
20. Why do you think co-transport is often called secondary active transport?
What is the advantage of such a type of transport?
21. Define the following: exocytosis, endocytosis, phagocytosis, pinocytosis, and
22. Know how many molecules of ATP, NADH, and FADH are generated (and which steps)
during cellular respiration in the presence and absence of oxygen.
23. What are redox reactions and what do they have to do with cellular
respiration or photosynthesis? Define oxidation, reduction, a reducting
agent, an oxidizing agent, an electron acceptor, and an electron donor.
24. Understand how the electron transport chain represent a controled release
of energy as 2H combines with 1/2 O2.
25. What are the two primary ways to synthesize ATP? Which is our predominant source
of ATP? If we accentuate or block on of these two ways of synthesis, be able to
calculate how many ATP could then be generated in X number of glucose molecules.
26. Know the component electron acceptors of the mitochondrial electron
transport chain. Compare the chloroplast electron transport chain with that
of the mitochondrial one? How are they similar but how are they distinct?
27. Why does FADH provide less energy than NADH?
28. Explain and fully comprehend Peter Mitchell's Chemiosmotic Hypothesis.
How does it operate in both animals and plants?
29. How are fats and proteins (in a general, global sense) catabolized?
30. What molecules act to upregulate or inhibit phosphofructokinase? Why
is this important? What is this principle called?
31. Define autotroph, heterotroph, consumer, producer, decomposer. What are
the 2 subdivisions of autotrophs?
32. Compare the net result of photosynthesis versus that of cellular
respiration in terms of chemical reactions as well as verbally.
33. Know where the atoms of the reactants of photosynthesis are incorporated
into the products.
34. What are the 2 stages of photosynthesis? Which is dependent upon light?
Which is dependent upon energy molecules. In which one is glucose actually
synthesized? What is the subcellular site of each of these two stages?
35. What is EMR and what portion of the light spectrum drives photosynthesis?
36. Explain using the absorption spectrum why plants are green? Of the three
pigments of photosynthesis, which do you suppose is of greatest concentration in
red algae? Why?
37. Understand the basis of Thomas Engelmann's algal-bacteria experiments.
38. Model the structure of a photosystem including, porphyrin ring, hydrocarbon
tail, the thylakoid membrane, the reaction center, the ground state, and the
exctied state. Where does the redox reaction occur? What replaces the lost
electron in chlorophyll a that is trapped in the primary electron acceptor?
39. Why are there two different routes of electron flow during the Light
Reaction? What are the component of these routes? What is produced and
how much during each of these routes?
40. Name three ways in which ATP synthesis in plants is different than that
of cellular respiration in mitochondria?
41. What are the 3 stages of the Calvin Reactions? How many molecules of CO2, ATP,
and NADPH must be consumed to generate 3 molecules of glucose?
Third Exam Study Questions:
1. Know what the major important contributions were by the following scientists:
Thomas Hunt Morgan, Gregor Mendel, Frederick Griffin, Oswald Avery, Alfred Hershey &
Martha Chase, Maurice Wilkins & Rosalind Franklin, Erwin Chargaff, James Watson &
Francis Crick, and Matthew Meselson & Franklin Stahl. Be able to describe the
experiments they set up, what the important equipment or tools were, what the
results of their experiment were, and how this information/data contributed to the
knowledge of the structure of dna or the method of genetic inheritance. For example,
describe two different experiments that were performed that made advantageous use
of radioactivity and what was discovered?
2. What is the difference between phenotype, genotype, allele, dominant trait,
3. How do we transform bacteria (e. coli) today differently than Griffin did in 1928? What
would be some typical goals of why we would want to transform e. coli?
4. Concerning the structure of DNA: how long is one helix turn? how far apart are
the nucleotide bases? how many layers of bases per helical turn? how wide is the
helix? why is this important for the arrangment of hydrogen bonding? how were all
these spacing/alignments discerned?
5. What does it mean that DNA has a 5' to 3' orientation? Be able to draw
this out and describe the phosphate versus hydroxyl end of the phosphate
sugar backbone and why we say the orientation is anti-parallel. What does it mean that
replication is semiconservative? What were two other theories of the day that
were rejected concerning DNA replication? How were they disproved?
6. How many base pairs are there in every individual cell and what is the error
rate during replication? How are errors corrected? What is a frame shift? What
is a single point mutation? What is a deletion? What is an insertion?
7. What is the difference between the replication fork, the replication bubble,
and the origin of repliction? Do the origin of replication exist on the parent
or the daughter strand? Are nucleotide bases added at the fork or the origin?
Does replication proceed at multiple sites or just one site? Is replication
taking place in one direction or does it move in both directions? How many nucleotide
can be added per second?
8. What is the name of the enzyme that adds nucleotide bases? How does it do so?
What is the leading strand versus the lagging strand? Why does one of these strands
produce Okazaki Fragments? What enzyme joins the fragments?
9. What is the role for the RNA primase and RNA primer for DNA replication? What
enzyme fills in the RNA from the primer with DNA bases? What is the function of
helicase and single-stranded binding protein?
10. What is meant by the statement: "Proteins are the link between the genotype
and the phenotype"? What is meant by the statement: "One gene-one polypeptide"?
11. How does transcription differ between prokaryotes and eukaryotes?
12. Define transcription versus translation? What are the three stages of each of
these and how do the events differ?
13. How is the primary transcript (pre-mRNA) altered through RNA processing to become
true mRNA (two ways)? How does this assist in the process of translation? What is the
evolutionary advantage of alternative RNA slicing? Where does RNA slicing take place?
What is exon shuffling? What is the difference between an exon and an intron?
14. Why must the genetic code be comprised of at least 3 nucleotides to create a
code for an amino acid? Define the following terms: codon, redundant code, anticodon,
stop codon, start codon.
15. If given a sequence of DNA and a mRNA codon table, be able to determine the
order of the resulting peptide. If given a peptide sequence and a mRNA codon table,
be able to provide a plausible sequence or sequences of DNA (remember redundancy) for
that peptide sequence. If told that there has been a particular mutation (an example
would be: insertion of a nucleotide at position X), be able to determine how this
will affect the production of the peptide.
16. What composes the transcription initiation complex? What are the individual
roles of the components of this complex? How does the template affect which
way the complex will move? Describe the steps of initiation, elongation, and
termination during transcription.
17. Know the functions of the following types of RNA: mRNA, tRNA, rRNA, pre mRNA
(primary transcript), snRNA, and SRP RNA.
18. What is the structure of a tRNA, naming two major structural motifs? What
enzyme catalyzes the phosphorylation of an amino acid to attach a particular
amino acid to the aa attachment site? What does the active site of the enzyme
have to do with the specificity of the anticodon?
19. What are the steps that occur during intiation of translation to assemble
the translation initiation complex? What are the roles of the mRNA, small subunit
of the ribosome, large subunit of the ribosome, initiation factor, GTP expenditure?
20. What are the formal names and functions of the E, P, and A sites? How many
GTP are expended to bind an incoming tRNA to the A site? What catalyzes the
formation of the peptide bond between the growing peptide chain and the new
incoming aa? What allows the tRNA to slide from positions P and A to positions
E and P?
21. What type of chemical reaction occurs when the release factor is bound
at the A site for the tRNA that has the anticodon for uga (stop codon)?
22. What is a chaperon protein and how does it assist protein function? How
does the polyribosome permit the synthesis of many copies of the same protein?
Click here for additional Third Hour Examination Questions and
Guide to Study for the Final Examination
Click here for additional Third Hour Examination Questions and
Guide to Study for the Final Examination