- Understand the basics of inorganic and organic
chemistry.
- Understand why proteins are vital to life.
- Be able to discuss the structure of an amino acid.
- Identify the properties of amino acids.
- Understand that proteins are polymers of amino acids.
- Understand that amino acid classification is based on
their ionic properties at physiological pH.
- Understand that protein structure is important to its
biological function.
- Understand the system of protein classification.
- Understand that animal s are
dependent on plants or other animals for their source of dietary protein.
- Understand chemical digestion of protein is a
catabolic process in which dietary protein molecules are broken down into
their monomers, amino acids
- Understand the metabolism of proteins
- Understand that enzymes are an important group of
proteins
- Understand that enzymes have unique characteristics
and properties.
- Understand how enzymes are named and classified
according to the type of reaction each catalyzes.
- Understand that many enzymes require a nonprotein component in order to function.
- Understand the role vitamins and minerals play as
enzyme cofactors.
- Understand that actors which influence the rate of an
enzymatic reaction and therefore control metabolic processes.
- Understand that enzymatic activities must be
controlled to ensure maintenance of homeostasis.
- Understand that inhibitors interfere with the action
of an enzyme and block or slow the rate of a reaction.
- Understand the role of enzymes as indictors of
disease.
- Understand that carbohydrates are extremely important
and abundant compounds in the biological world.
- Understand the expenditure if energy through
mechanical work and biochemical reaction requires that organisms have
available a constant supply of energy.
- Understand that carbohydrates supply approximately 50%
of the total calories or energy value.
- Understand the importance of maintaining the blood
glucose level.
- Understand that lipids are a chemically divers group
of organic compounds essential to life.
2.
Some
review of Chemistry stuff (from chemistry handout/notes):
|
|
What are the four most commonly
occurring elements? |
|
|
Review atomic structure |
|
|
What is the difference between
covalent bonds, ionic bonds and hydrogen bonds? |
|
|
What type of bonds link atoms
together to form molecules? |
|
|
Why is carbon central on
biological molecules? |
|
|
What is a carbon skeleton? |
|
|
How many bonds can Carbon form
with other atoms? |
|
|
How many bonds can Hydrogen form
with other atoms? |
|
|
How many bonds can Oxygen form
with other atoms? |
|
|
What are functional groups? |
|
|
Be able to recognize or draw
certain functional groups |
|
|
Hydroxyl (alcohol), carboxyl,
amino, carbonyl |
|
|
be able to recognize the reactants
and products in a chemical reaction |
|
|
Know and be able to list the four
types of biological macromolecules. |
|
|
What is a polymer? A monomer? |
|
|
review
dehydration synthesis and hydrolysis. Know if a water molecule is formed or
used. Think about how many water molecules would be used /produced in a
polymer of different sizes. |
3.
Chapter 7 (18): Carbohydrates
|
|
What are dietary sources of
carbohydrates? |
|
|
Be able to give specific
examples of functions of carbohydrates in the body (for example saying
"cell membrane" is not a function). Also, be able to come up with a
non-energy related function. |
|
|
What are the functions of
carbohydrates in our everyday lives? |
|
|
What functional groups are found
in carbohydrates? |
|
|
Which of the four most commonly
occurring elements are found in carbs? Which are not? |
|
|
Be able to distinguish an aldehyde
from a ketone group on a carbohydrate |
|
|
What is a stereoisomer/entaniomer? What monosaccharide isomer is found in
humans? |
|
|
Be able to recognize the
difference between the D and L isomers in a structural formula. |
|
|
What is meant by dextrotatory and levorotatory molecules? How are they
distinguished? |
|
|
How are monosaccharides
classified? |
|
|
What is the difference between a
triose, tetrose, pentose, etc.
Be able to give examples we discussed in class. |
|
|
What are the most common 6-carbon monosaccharides? |
|
|
What is the general chemical
(molecular) formula for glucose, fructose and galactose?
Review info about these three monosaccharides. |
|
|
What happens when a monosaccharide
is placed in an aqueous solution? |
|
|
Be able to draw glucose in either
a ring or straight (linear) form |
|
|
Be able to draw the formation of a
glycoside bond ( p. 262 (p. 538) |
|
|
Be able to draw or recognize a
generic carbohydrate given its name (ex: aldopentose)
like we did on the in-class worksheet |
|
|
|
How are monosaccharides
linked together to form polysaccharides? Be able to draw this process. |
|
|
Review dehydration synthesis. What
does it do? Are water molecules used or produced? |
|
|
Review hydrolysis. What does it
do? Are water molecules used or produced? |
|
|
What is a glycoside bond? |
|
|
Be able to distinguish between an
alpha 1-4 glycoside bond and a beta 1-4 glycoside bond. Which disscharides/polymers have which type of bond? How does
the difference it affect shape/function/properties? What is the significance
to the human diet? |
|
|
Review the 4 disaccharides that we
discussed in class. Know what the component monosaccharides
are, and some basic facts about each. What type of bond holds them together?
What is the general chemical (molecular) formula for a disaccharide? |
|
|
review lactose intolerance |
|
|
What enzymes break each of the
disaccharides? |
|
|
Carbohydrates made up of simple
sugar monomers called monosaccharides
(glucose in particular). |
|
|
Know the structure and functions
of the following polysaccharides and also how they differ from one another. (are they found in animals or plants? are they soluble in
water? are they structural molecules or glucose storage molecules? is it
digestible by humans? ) |
7.
Starch
(amylose and amylopectin)
Glycogen
Cellulose
Chitin
|
|
How
can someone test for the presence of starch? Would this test also work for
glucose? |
|
|
What is glycogenesis? Glycogenolysis? |
|
|
what is the role of fiber in
the diet? |
|
|
What are the acidic
polysaccharides? What are their functions? |
|
|
What are oligosaccharides? |
|
|
What are glycolipids and
glycoproteins? |
8.
From
the text, questions you should be able to answer from ch
7 (answers to odd #'d questions are in back of the book)
9.
1,3,
7-14, 17-20, 23, 25, 33,34,37-40, 41-44, 49, 50, 53, 54, 57,91, 92, 106-127,
134, 137-141, 144-148
10. From the text, questions you
should be able to answer from ch 18 (answers to odd
#'d questions are in back of the book)
11. 1-4, 7-14, 17-20, 23, 29,
33,34,37 -40,49, 50, 53, 59, 60, 87-88, 93, 101-115, 118, 122, 125-127, 130
-134
12.
Lipids
|
|
Lipids are macromolecules but are
NOT polymers |
|
|
Be familiar with the functions of
lipids |
|
|
Be familiar with the common
properties of lipids |
|
|
What elements make up lipids? How
is this different than carbohydrates and proteins? |
|
|
All lipids are hydrophobic (or
amphipathic) what is meant by amphipathic? |
|
|
Be able to recognize a fatty acid
structure. |
|
|
Know the difference between
unsaturated and saturated fatty acids. (in terms of both structure and
properties) |
|
|
Be familiar with the difference
between monounsaturated and polyunsaturated. |
|
|
What are examples of lipids (in
our diet) that contain each? |
|
|
What is meant by the cis and trans isomers of fatty acids? Where
do each occur? Which is more similar to a saturated
fatty acid? what does hydrogenation mean? |
|
|
What is the difference between omega
3 and omega 6 fatty acids in terms of structure? What about in the diet? |
|
|
be able to write the abbreviation
for a given fatty acid (for example, 18:2D6,
9) |
|
|
Be familiar with the five
categories of Lipids. What is an example of each? Be able to match a lipid to
its category. |
|
|
What are Triacylglycerols?
What are their functions? |
|
|
What is the structure of a
triacylglycerol? Be able to recognize. |
|
|
How are triacylglycerols
formed from their components? How many water molecules are involved? What
type of linkage hold the fatty acids to the glycerol? |
|
|
What is the different between fats
and oils? |
|
|
What are the dietary sources of
fats and oils?What are
sources of both "bad' and "good" fats and oils? |
|
|
What is meant by the term
"essential"? essential fatty acids/ What
are the two essential fatty acids? Where can we get them in our diet? |
|
|
How are lipids different that the
other classes of macromolecules that we have discussed? |
|
|
What are the three types of
Membrane Lipids? How many fatty acids do they each contain? |
|
|
What are phospholipids composed
of? which part of the molecule is hydrophilic? hydrophobic? What is the difference between a phospholipid
and a sphingophospholipid? What is the difference
between a phospholipid and a sphingoglycolipid? Be
able to recognize these structures |
|
|
what
is the general structure of cholesterol? What is its function in the cell
membrane? |
|
|
How do the three types of membrane
lipids come together to form the plasma membrane? How are the lipids
arranged? What other macromolecules are part of the
membrane? |
|
|
Be able to draw a schematic of the
different types of membrane lipids (as on page 314/584) and label the
different parts. |
|
|
What is an emulsifier? What abut the structure of bile acids allow them to act as an
emulsifier? Where are bile acids made and stored? |
|
|
Messenger Lipids: Steroid
hormones/eicosanoids |
|
|
What are examples of steroid
hormones? What are they derived from? |
|
|
What is the difference between how
steroids and eicosanoids work? |
|
|
What are examples of eicosanoids? |
|
|
How do drugs such as
aspirin/ibuprofen/advair work? |
|
|
What are are
examples of Waxes? |
|
|
What are waxes composed of? |
|
|
Which lipids contain fatty acids?
How many fatty acids? |
|
|
Be familiar with the components/parts
that make up the different types of lipids. |
|
|
Review summary table at the end of
the chapter |
15.
In book, questions you should be
comfortable with:
16.
New edition:
17.
p. 292 ex 8.1
p. 307 ex 8.4 a, c (in yellow box)
18.
back of chapter questions
19.
1,5, 6, 9-14, 25, 26, 39-44, 45a,
64-66, 69-72, 77, 79, 85-90, 92, 99, 107, 110ac, 121, 122, 123, 127-131,
134-136, 138-139, 141, 142
20.
old edition:
21.
p 565 ex 19.1
p 578 ex 19.2 a, c (in yellow box)
back of chapter questions:19.1, 19.5, 19.6, 19.9, 19.10, 19.11, 19.12, 19.13,
19.14, 19.17, 19.23, 19.37, 19.39, 19.41, 19.61-64, 19.67-70, 19.76, 19.77,
19.85, 19.87, 19.101, 19.103-104, 19.114, 19.115, 19.116, 19.118, 19.119
22.
Proteins
|
|
What are the monomers that make up
proteins? |
|
|
What are the parts of amino acids? |
|
|
Be able to recognize and draw the
general structure of an amino acid. |
|
|
Be able to draw and identify
the properties of (is it hydrophobic? hydrophilic? acidic? basic?) the
following amino acids: Alanine, Leucine, Glycine,
Cysteine, Tyrosine, Glutamic acid, Lysine |
|
|
How many different amino acids are
there? |
|
|
What elements make up proteins? |
|
|
What is an
enantiomer/stereoisomer? What amino acid stereoisomer is found in humans? |
|
|
Ionization of an amino acid can
occur at the amino group, the carboxyl group or both, depending on the pH |
|
|
Review how amino acids will ionize
(which groups are charged?) at low pH, high pH, physiological
pH. |
|
|
What is meant by essential amino
acids? |
|
|
How are amino acids linked
together to form polypeptides? |
|
|
Review dehydration synthesis. What
does it do? Are water molecules used or produced? |
|
|
Review hydrolysis. What does it
do? Are water molecules used or produced? |
|
|
What is a peptide bond? |
|
|
Be able to draw the formation of a
peptide bond |
|
|
Know the way to name small
peptides |
|
|
Know the difference between the
primary structure of a protein and the higher order structures (secondary,
tertiary and quaternary) |
|
|
Primary |
|
|
Secondary |
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|
Tertiary |
|
|
Quaternary |
|
|
Be able to recognize which level
of structure in a drawing |
|
|
What are simple proteins? |
|
|
What are conjugated proteins? Be
familiar with the sub-groups of conjugated proteins What is a prosthetic
group? |
|
|
What is denaturation? What can
cause denaturation? |
|
|
What are some important functions
for proteins in our cells? Be able to either list or match functions with
examples discussed in class. |
|
|
What is the difference between
fibrous and globular proteins? What are some examples of each? |
|
|
What is denaturation? What types
of structure is disrupted? |
|
|
What are examples of denaturing
agents and how do they work? |
|
|
|
27.
New edition:
28.
p. 340 ex 9.1
p. 345 ex 9.3
p. 346 ex 9.4
p. 356 ex 9.5
29.
back of chapter questions
30.
1, 2, 7, 11, 21, 22, 27acd, 30,
39-52, 55, 56, 63-69, 71, 75-86, 89-98, 105-108
31.
old edition :
32.
In book, questions you should be
comfortable with:
33.
p 609 example 20.1
p 614 example 20.3
34.
questions at the end of the chapter
(I will just type in 11, rather than 20.11 for example)
35.
4, 7, 8, 23 a, c, d, 26, 35, 37, 40,
47, 63, 64, 65, 69, 71, 75, 76, 77, 81, 89,
Chapter
10 (21): Enzymes
- Enzymes catalyze
biological reactions
- What types of
macromolecule are enzymes?
- Describe the mechanism
of enzyme action
- how do enzymes accelerate
reactions?
- Be familiar with the
terms substrate, enzyme-substrate complex, product, active site,
transition state
- What is activation
energy? What effect do enzymes have on this?
- what is the transition
state?
- What is an active site?
How does the substrate interact with the enzyme? What types of bonds are
involved?
- Enzymes lower activation
energy for reactions
- Enzyme specificity
(Absolute or relative)--what is the difference?
- Review notes on
lactose/lactase
- Be familiar with the
Lock and Key versus Induced Fit models of substrate/enzyme interaction
- What is the difference
between simple and conjugated enzymes?
- What is a cofactor?
|
|
|
|
What is an apoenzyme?
Holoenzyme? |
|
|
Enzyme names end in –ase |
|
|
Be familiar with the following general types of enzymes and
what they do: |
|
|
Be familiar with alcohol dehydrogenase because we used this
example repeatedly |
|
ethylene
glycol -à glycolic and oxalic acids (see info on
competitive inhibitors below) |
|
|
|
metal ion cofactor: zinc |
|
|
coenzyme:
NAD+ |
- What
are factors that influence enzyme activity?
- review graphs we discussed in
class looking at the effect of pH, temp, substrate conc., enzyme conc.,
end product conc. on reaction rates.
- what is meant by optimum ph? optimum temperature?
- review your in-class handout.
- Be able to draw a graph
given some information on these factors.
Enzyme Inhibition
- Irreversible
- Change tertiary or
quaternary structure if enzyme/permanently inactivates
- Example: insecticides,
nerve gas, penicillin, cyanide
- How do each if these
work (what enzyme is inactivated?)
Reversible
Competitive
·
Structurally similar to natural substrate/compete with it for
binding to active site
·
Examples:1.ethylene glycol is competitive inhibitor of
alcohol dehydrogenase (see reaction above) and 2.sulfa drugs
Non-competitive
·
Do not resemble substrate/bind away from active site
·
Examples: heavy metal ions (lead/mercury)
Enzyme
regulation
reviewgenetic control of enzyme activity. Ex: lactose metabolism genes- Allosteric regulation
When is this involved? How does it work? Where does regulator bind? - Zymogens
- What is a zymogen?
- Examples: pepsinogen, trypsinogen, prothrombin,
fibrinogen
Be
able to answer the following questions from the end of chapter 10:
1-3, 4-18,
21-22, 25-34, 37-43, 47-53, 57-58, 65-68, 103, 111-117
Be
able to answer the following questions from the end of chapter 21:
1-6, 9-12,
19-26, 29-32, 35-43, 45-47, 49-60
Chapter
11 (22): Nucleic Acids
DNA Structure
|
|
G, A, T, C = 4 nucleotides (monomers) that
make up DNA |
|
|
What are the three components of a nucleotide? |
|
|
Nucleotides joined by dehydration
synthesis--bond holding nucleotides together along chain are phosphodiester bonds. Watson
Crick model: Nucleotides are linked together (using dehydration synthesis
reactions, of course!) to make a chain; two chains are held together by weak
hydrogen bonds to make a double stranded helical molecule. |
|
|
A always pairs with T; G always pairs with C |
|
|
Be able to determine the second DNA strand if
given a single strand of DNA |
|
|
RNA nucleotides = G, A, U, and C. What are the
differences between DNA and RNA? |
DNA to Proteins
- DNA ---->RNA----->Protein
- DNA, which contains genetic information, is stored in nucleus
What is DNA Polymerase? What does it do?- DNA is copied during TRANSCRIPTION into mRNA which can leave
the nucleus
|
|
A new RNA is copied from a specific DNA region
according to base-pairing rules during transcription . What is the
enzyme that catalyzes the formation of mRNA? |
|
|
The information on mRNA is TRANSLATED into
protein in the cytoplasm |
|
|
*Be able to make an mRNA sequence if given a
DNA sequence, and the be able to
"translate" this mRNA into protein using the genetic code. (Like
the in-class exercise) |
|
|
AUG = start codon |
|
|
what
is a codon? |
What
is rRNA? Where is it found?
what is tRNA? How is it
involved in translation?
What is an anticodon? Where is it found? what does it
do?
Where is the amino acid attached to the tRNA?
What is the role of the ribosome in translation?
Review the steps of translation as shown in figure 11-22 (22.22) and 11-23
(22.23)
Be
able to answer the following questions from the end of chapter 11:
3-6,
8-12, 25-26, 35-39, 45-45, 50, 57-60, 67-72, 79-80, 85-88, 93-96, 99-102, 105,
110, 115-116, 140, 147, 150-152, 154-155
Be
able to answer the following questions from the end of chapter 22:
2,
4, 11, 12, 15, 16, 19, 20, 25-29, 35-38, 47, 53, 58, 71-82, 85-88, 90, 93, 94,
118, 121, 125, 128-130, 132, 133