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CHAPTER 1
After reading the relevant parts of the text, one should be
able to:
1. Briefly describe the unifying themes that are present in Biology
Pages 1-14; see fig. 1.3 p 5
2. Diagram the hierarchy of structural levels in Biology
Pages 3-4
3. What is an emergent property? A new property that arises
as life increases in the structural level of life. P.4
3. What are some of the properties and processes we associate
w/ the state of being alive?
p. 6 fig. 1.3; same thing as "defining features"
of life as presented in lecture.
4. What is the lowest level of structure capable of performing
all activities of life? p. 4-5
5. What is the continuity of life based on? Fig. 1.5
6. Do all forms of life use the same genetic code? P 6&7
7. What branch of science deals w/ the classification of life?
Understand all terms listed in fig. 1.10.
8. A famous quote by a prominent biologist is "Nothing in
Biology makes sense except in the light of evolution". What
is Evolution how does it account for both the unity, and the diversity
of life? P.12 and 13
TERMS YOU SHOULD KNOW
| matter | electron | covalent bond | atomic # & Mass # |
| electron shell | polar covalent bond | non-polar covalent | element |
| ionic bond | valence | electron | radioactive isotope |
| chemical bond | isotope | half life | electronegativity |
| proton & neutron | hydrogen bond | polar |
MORE CHAPTER 2 INFO
1. Do electron's contribute significantly to the atomic mass
of an atom? p. 25
2. What is the difference between a stable isotope and an unstable
(radioactive isotope)? p. 25
3. Is and atom's nucleus involved in chemical reactions between
atoms?
4. Which is more reactive, and atom with a full valence shell
or an atom w/ a partially full valence shell? p. 27.
5. How does electronegativity play a part in ionic bond formation?
p. 29.
6. Do the self-quiz questions-
#1; #3; #5; #6; #7;
CHAPTER 3
WATER AND THE FITNESS OF THE ENVIRONMENT
LEARNING OBJECTIVES-
After attending lecture and reading the relevant sections of the
text, the student should be able to:
1. Describe how water contributes to the fitness of the environment
to support life.
2. Describe the structure of water molecules, and explain what
properties emerge as a result of this structure.
3. Explain the relationship between the polar nature of water
and its ability to form hydrogen bonds.
4. Explain how acids and bases directly or indirectly affect [H+]
of a solution.
5. How do buffers work? Describe using the bicarbonate buffer
system as an example.
6. Explain the pH scale.
7. What are the properties of water that make life, as we know
it possible?
KEY TERMS-
Heat of vaporization; evaporative cooling; solution; solvent;
hydroxide ion; hydrogen ion; acid; base; pH scale; buffer; specific
heat
MORE CHAPTER 3 INFO
1. Water molecules are held together by Hydrogen bonding.
What characteristics of water's chemical structure allow hydrogen
bonding to occur? p. 37.
2. Water molecules stick together by H-bonding. Are the hydrogen
bonds permanent or fleeting? Why does water have more structure
than most other liquids? p. 38.
3. Why does ice float? P40-41. How does ice formation increase
the fitness (habitability) of the environment? Fig. 3.6
4. Understand figures 3.7 & 3.8
5. Don't do any of the self-quiz questions; they're pretty bad
and don't correlate well with lecture.
CHAPTER 4
OBJECTIVES-
After attending lecture and reading the relevant sections
of the text, the student should be able to:
1. Explain how carbon's electron configuration determines the
kinds and number of bonds carbon will form.
2. Describe how carbon skeletons vary
3. Recognize the major functional groups, and describe the chemical
properties of organic molecules in which they occur.
KEY TERMS-
organic molecule functional group hydroxyl alcohol
carbonyl carboxyl carboxylic acid amino group
amine phosphate group hydrocarbon
MORE CHAPTER 4 INFO
1. Be able to recognize diagrams of all functional groups
discussed in lecture. Table 4.1 p54
2. Why is a carboxyl group considered to be acidic? p. 55 4. Read
the chemical elements of life: a review p. 61.
3. Study fig. 4.4 to understand the molecular diversity of carbon
skeletons.
Do the self-quiz questions-
#1; #3; #7; #8; #9
KEY TERMS - CHAPTER 5
polymer glycogen protein denaturation
monomer cellulose amino acid nucleic acid
macromolecule chitin polypeptide nucleotide
condensation reaction peptide bond hydrolysis protein conformation
carbohydrate lipid monosaccharide fat
primary structure DNA dissaccharide phospholipid
RNA polysaccharide steroid tertiary structure
pentose quaternary structure starch triglyceride
disulfide bridge secondary structure
After attending lecture and reading your text, the student should
be able to:
1. describe how covalent bonds are formed and broken in organic
polymers
2. describe the distinguishing characteristics of carbohydrates,
and explain how they are classified.
3. Describe the important biological functions of polysaccharides
4. Distinguish between starch, glycogen, cellulose, and chitin.
5. Explain what distinguishes lipids from other macromolecules
6. Describe the unique properties, building blocks and biological
importance of the three groups of lipids: fats, phospholipids
and steroids
7. Describe the difference between unsaturated and saturated fats
8. Describe the characteristics that distinguish proteins from
the other major classes of macromolecules, and explain the biologically
important functions of this group.
9. List and recognize the four major components of an amino acid,
and explain how amino acids may be grouped according to the physical
and chemical properties of the side chains.
10. Identify a peptide bond and explain how it is formed.
11. Explain what determines protein conformation
12. What is primary structure?
13. Describe the 2 types of secondary structure and explain the
role of hydrogen bonds.
14. Describe tertiary structure
15. Describe quaternary protein structure
16. What is denaturation and explain how proteins can be denatured.
CHAPTER 5
1. Be able to recognize diagrams of all polymers and monomers
discussed in lecture.
2. Why are scientist's interested in the structure of macromolecules?
FIG. 5.1
3. See Fig. 5.3 What makes a monosaccharide a monosaccharide?
4.. Fig. 5.2 Understand how biomolecules are synthesized
and broken down.
5. See f. 5.6 - Be able to compare and contrast glycogen and starch;
what chemical process releases glucose molecules, from starch
or glycogen, to a plant or an animal? Is glycogen good for long
term energy storage? p. 68.
6. Why can't we digest cellulose w/ our enzymes? P. 63
7. How does chitin's monomer subunit differ compared to most other
monomers of carbohydrates? p64 and 65
8. See f. 5.10 structure of a fat.
9. The heads of fat are made of carboxylic acids, which are polar.
Then why is fat hydrophobic?
10. F. 5.11 - Why are saturated fats solids at room temperature?
11. Why do phospholipids make great components for cell membranes?
P67&68f. 5.13
12. See Fig. 5.14 + read cholesterol info on P68.
13. What is the general formula for an amino acid? P68.
14. Understand the four levels of protein structure. See Figures
5.18, 5.20, 5.22, and 5.23.
15. What are some of the functions a proteins? table 5.1 Cite
the function plus give one example.
16. What are the four categories of amino acids? P69 What component
of an amino acid is used for the basis of the 4 categories?
17. See Fig. 5.25. What does the term denaturation mean? What
kinds of environmental factors can denature a protein?
18. Be able to recognize the correct location of peptide bonds
in a polypeptide!!!!!! P70
19. Do the self quiz questions- #1; #2; #3; #5; #6
CHAPTER 6
TERMS
metabolism catabolic pw's anabolic pw's catalyst
enzyme Ea (activation NRG) substrate active site
induced fit saturated competitive inhibitors noncompetitive inhibitors
cooperativity allosteric site feedback inhibition
1. Why are the phosphate bonds of ATP considered to be high
energy? p. 96
2. From what chemical source is ATP regenerated from? Where does
the energy come from to drive the regeneration of ATP? fig. 6.8
p. 97
3. Understand f. 6.9!!!!!! If you don't understand this, you won't
understand how an enzyme catalylizes a reaction!! See fig. 6.10.
4. How many substrate molecules can an enzyme process per second?
p. 99
5. The degree of inhibition can vary. What determines wether or
not a chemical inhibitor is reversible or nonreversible?
6. What does induced fit mean? fig. 6.11.
7. Is inhibition of an enzyme always a bad thing? hint: allosteric
regulation p. 101 and 102.
8. do the self quiz questions-
#3; #5; #6; #7; #8; Challenge question #2
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