CHAPTER 19 – CARBOHYDRATES
After achieving the learning objectives of this chapter, you will be
able to:
Section 19.1 & 21. Define the
following terms and give an example of each: carbohydrate, monosaccharide, aldose, ketose, hexose, pentose, and amino sugars. (19.8, 19.10) 2. Identify chiral carbons in the Fisher projection of a monosaccharide, determine whether it is D or L form. (19.13) 3. Identify the
enantiomers and diastereomers
of D-glucose. (19.16) Sections 19.3 & 19.44. Draw the 5. Describe the
following structures of D-glucose in water: open-chain form, alpha-D-glucose,
and beta-D-glucose. Number the carbon atoms in each form.(19.24) 6. Describe how
to classify sugars as to whether they are reducing or non-reducing sugars.
Give an example of each class. 7. Draw the
structure of a disaccharide joined by a glycosic
linkage of two monosaccharides. Label the
linkage by carbon number and anomer type. (19.34,
19.42, 19.44, 19.67). 8. Give an
example of each of the following class of compounds, point out how their
chemical structures relate to Monosaccharides, and
a major biological function of each: (a) alditols,
(b) Adonic acids, and (c) uronic
acids. Sections 19.5, 6 & 79. Differentiate
these terms and give an example of each: disaccharide, oligosaccharide, and
polysaccharide 10. Prepare a
table summarizing characteristics of the following: maltose, lactose,
sucrose, starch, cellulose, hyaluronic acid,
heparin in terms of: (a) natural occurrence, (b) biological function(s), (c)
monosaccharide components, (d) type(s) of glycosidic
linkage. CHAPTER 20 - LIPIDS After completing this chapter
you should be able to: 1.
Define the term lipid and recognize the different
classes of lipids upon looking at their structure; give actual examples of
each class. (sec 20.1) (exercise
20.3) 2.
Draw the structure of a fat molecule and explain
the terms: triglycerides or triacylglycerol, and di- or mono-glyceride. (sec
20.2) (exercise 20.4) 3.
Compare and contrast saturated and unsaturated
fatty acids, including monounsaturated and polyunsaturated fatty acids. (sec
20.2) (exercise 20.5) 4.
Tell the structural characteristics of fatty
acids. (sec 20.2) 5.
Discuss the following chemical and physical
properties of fatty acids: (a) pH sensitivity, (b) solubility, (c) melting
point, (d) hydrogenation reactions, and (e) oxidation reactions. (Lecture
notes, sec 20.2,3) (exercise 20.8) 6.
Write equations to show the formation of fat from
glycerol and fatty acids.(Lecture notes) 7.
Tell what distinguishes a fat from oil in terms of
physical properties and molecular structures. (sec 20.3) (exercise
20.11, 20.13) 8.
Write equations to show the hydrogenation
of unsaturated fat into saturated fat.(Lecture notes, sec 20.3) (exercise
20.14) 9.
Explain the term saponification;
tell how soap works. (sec 20.3) (exercise 20.15, 20.16) 10. Describe the
general structure of complex lipids: phospholipids, sphingolipids,
glycolipids. Give an
actual example of each type with its biological functions. (sec 20.4,6,7,8) (exercise
20.21,20.26) 11. Describe the
fluid mosaic model of cell membranes, listing components in order of relative
amount present. (sec 20.5) (exercise 20.17,20.19) 12. Describe
typical molecular structures of: micelles and lipid bilayers.
Give examples of biological functions of each. (sec 20.5, LAP NF.6) 13. Describe the
general structure of steroids and lipoproteins. (sec 20.9, LAP NF.6) 14. Describe
cholesterol, HDL and LDL, respectively, in terms of (a) chemical structure,
(b) biological functions,
and (c) relationship with atherosclerosis. (LAP NF.5, sec 20.9)
(exercise 20.27, 20.29, 20.31, 20.33) 15. Name two
major types of steroid hormones and discuss the major functions of each. (sec
20.10)(exercise 20.43, 20.44) 16. explain the function of bile acids. Give examples. (sec 20.11) (exercise
20.24) 17. Discuss two
types of eicosanoids and the major function
of each. (sec 20.12)(exercise 20.45, 20.48) 18. Tell what
the term "essential fatty acid" mean and give an example.
(LAP NF.4) CHAPTER 21 – PROTEINS
After completing this chapter, you should
be able to:
1.
List the various types of proteins, describe their
functions and give an actual example of each one. (sec 21.1) (exercise 21.4) 2.
Describe each of the following terms and tell the
relationship between them: amino acid, peptide, and protein. (sec 21.2) 3.
List by memory the names and abbreviations of all
the amino acids commonly found in proteins in each of the four categories
given in Table 21.1. (Exercise 21.6) 4.
Classify an amino acid to one of four type when given its structure. (sec 21.3 ) (exercise 21.9, 21.10) 5.
Explain the term “zwitterions” and give examples.
(sec 21.3) (exercise 21.18) 6.
Explain what the isoelectric
point of an amino acid is and tell the relationship between pH and pI. (sec 21.3) 7.
Draw structures of an amino acid at low, medium
and high pH environments, respectively, given its pI
value(s). (sec 21.3) (Exercise 21.19) 8. Describe the “handedness” of amino acids; draw the D and L forms of any amino acid; and tell which exists in nature. (lecture notes) (Exercise 21.8, 21.12, 21.15) 9. Draw the structure of cysteine and cystine. Describe the condition under which they inter-convert. (sec 21.4) 10. Describe the
structure of a peptide bond in terms of geometry, polarity and possible
hydrogen bonding location(s). (Lecture notes) (Exercise 21.26) 11. Draw
structures of dipeptides and polypeptides when
given the amino acids. Identify peptide bonds, amino acid residues and R
groups in a dipeptide or polypeptide. (sec 21.5) (Exercise
21.20, 21.22, 21.23, 21.25, 21.27) 12. Describe the four levels of protein structures and specify the chemical bonds or forces holding each structure. (sec 21.6,7) 13. Give one
actual example showing the importance of amino acid sequence in protein
structure and function. (sec 21.7) (Exercise 21.30, 21.40) 14. Sketch a
section of helix and of sheet protein structure, respectively. Explain how
these structures are maintained by hydrogen bonding. (sec 21.8) (Exercise
21.36) 15. Discuss the
four ways by which tertiary protein structures are stabilized. (sec 21.10) (Exercise
21.35, 21.37, 21.39) 16. Discuss the
special quaternary structures of each of these proteins in relation to their
specific functions in the body: hemoglobin, collagen and integral membrane
protein. (sec 21.9) (Exercise 21.42) 17. Discuss glycoproteins in terms of structure and function in the
body. (sec 21.10) (Exercise 21.47, 21.49) 18. Tell the
differences between a native protein and a denatured protein. List several
ways to denature proteins and explain how each works. (sec21.11) (Exercise
21.41) 19. Explain the
acid/base properties of proteins; tell how pH relates to protein structure.
(Lecture notes) (Exercise 21.28) 20. Describe the
gel electrophoresis technique and how it is applied in serum protein
analysis. (lab) 21. List the essential
amino acids by name. Explain how essential amino acids relate to complete
proteins. (LAP NF.8) CHAPTER 22 – ENZYMES After completing this chapter, you should
be able to:
1. Define the
term: “enzyme specificity” and discuss different types of specificity. (sec
22.1) (Exercise 22.3,22.5, 22.6) 2. Name the main
classes of enzymes (sec 22.2, Table 22.1) and recognize what category
an enzyme belongs to when given the reaction it catalyzes. (lecture notes) (Exercise
22.7, 22.9,22.10) 3. Define each
term and give an example of each: coenzyme, active site, substrate,
competitive inhibitor, noncompetitive inhibitor, activation and inhibition
in relation to an enzyme. (sec 22.3) (Exercise 22.12) 4. Describe the
effect of enzyme and substrate concentration on enzyme activity and represent
this relationship graphically (sec 22.4) (Exercise 22.15) 5. Describe the
effect of temperature and pH on enzyme activity and show graphically how enzyme activity
varies as we change these two variables. (sec 22.4) (Exercise 22.16,
22.17, 22.19) 6. Compare and
contrast the lock and key model of enzyme action and the induced
fit model. Explain the types of
forces are involved in the formation of the E-S complex in these models. (sec
22.5) (Exercise 22.21, 22.22, 22.23, 22.24) 7. Describe competitive,
non-competitive and irreversible inhibition of enzymes as
follows: (a) Give examples of each type of inhibition, (b) Represent these
processes graphically of competitive versus non-competitive inhibition, and
(c) Predict how the end result of an enzyme catalyzed reaction is affected in
each type of inhibition by increasing substrate concentration. (sec 22.5) (Exercise
22.25) 8. Describe the
five mechanisms of enzyme regulation and briefly describe each one. (sec
22.6) (Exercise 22.33) 9. Differentiate
the two processes of enzyme regulation: feedback and allosteric
control. (sec 22.6) (Exercise 22.27, 22.28) 10. Explain how proenzyme and zymogen relate to
the function of an enzyme. Give examples. (sec 22.6) (Exercise 22.30) 11. Describe one
actual example of enzyme assays used in medical diagnosis. (sec 22.7, Table
22.2) CHAPTER 23 – CHEMICAL
COMMUNICATIONS: NEUROTRANSMITTERS AND HORMONES
After completing this chapter, you should
be able to:
1. Compare and
contrast the two types of chemical messengers involved in cell communication
by listing separately the similarities and differences of the two in terms of
(a) how each is produced, (b) how each works. (sec 23.1) (Exercise
23.6) 2. Describe the
endocrine system and explain how the hypothalamus communicates with other
tissues. (sec 23.2, FIG 23.2) 3. Describe
what a neuron looks like, or name its parts given a diagram. (FIG 23.1) (Exercise
23.4) 4. Define the
terms agonist and antagonist and explain how drugs can act as either one of
these. (sec 23.1) 5. Name five
classes of chemical messengers and explain the mode of action of each. (sec
23.2) (Exercise 23.8) 6. Explain how
acetylcholine works as a neurotransmitter. (sec 23.3)(Exercise 23.10) 7. Describe the
mode of actions of several different drugs and toxins that act as
acetylcholine agonists or antagonists. (lecture notes, sec 23.3) (Exercise
23.11) 8. Describe/explain
the mode of action of adrenergic messengers (epinephrine & others).
Describe/explain the “signal transduction” process and the use of “second messengers”.
(sec 23.5) (Exercise 23.18, 23.19, 23.21, 23.24, 23.25) 9. Explain how
histamine and antihistamine work. (sec 23.5) 10. Discuss the
role of neuropeptides in pain relief. (sec 23.6) (Exercise
23.29, 23.31) CHAPTER 24 – NUCLEOTIDES, NUCLEIC ACIDS, AND
HEREDITY After
completing this chapter you should be able to: 1. State what DNA and RNA stand for and show how they relate to each of the following: chromosome, gene, nucleic acid, nucleotide, and nucleoside. (sec 24.1) (Exercise 24.4,24.5,24.12) 2. Identify the three parts of a nucleotide when given its structure; when given the structures of the three parts individually, draw the structure of the nucleotide. (sec 24.2) (exercise 24.9, 24.15,24.16) 3. Recognize
the structure of adenine, guanine, cytosine, thymine, and uracil.
Given the structure, classify each base as a purine
or pyrimidine. (sec 24..2) (exercise 24.8,
24.10) 4. Draw and name a DNA or RNA segment when the base sequence is given. Mark the 3’ and 5’ ends, and identify the phosphoester bonds, sugar and base segments. (sec 24.3)(exercise 24.17) 5. Draw
hydrogen bonded base pairs with the correct number and placement of hydrogen
bonds given the structures of the bases. (Figure 24.5, 24.7) (exercise 24.19) 6. Explain the
meaning of each phrase, noting particularly the words in quotes: (a) DNA
“double helix,” (b) “antiparallel” DNA strands, and
(c) “complementary” base pairing. (sec 24.3) 7. Compare and contrast major structural differences between DNA and RNA. (sec 24.3 and 24.5) 8. List the functions of the three types of cellular RNA. (sec 24.4) (exercise 24.25, 24.27, 24.32) 9. Describe DNA replication step-by-step (how it starts,
proceeds, ends; which enzyme / molecule is involved for what purpose, and how
to ensure accuracy of the process). Include the meaning of these terms in
your description: (a) semi-conservative, (b) lagging strand, (c) leading
strand, (d) replication fork, (e) primers, (f) 10. Describe an
example of DNA repair process. (sec 24.7) (exercise 24.51, 24.52) 11. Define the
terms: cloning, molecular cloing and PCR. (sec
24.8) CHAPTER 25 – GENE EXPRESSION AND PROTEIN
SYNTHESIS After
completing this chapter you should be able to: 1. State the
central dogma of molecular genetics. (sec 25.1) 2. Define the
term: gene expression. (sec 25.1) (exercise 25.5) 3. Describe the transcription process to make RNA (how it starts, proceeds, ends; which enzyme / molecule is involved for what purpose). Include the meaning of these terms in your description: (a) template strand, (b) informational strand, (c) where transcription occurs in the cell, (d) intron, (e) exon, (f) structural gene, (g) regulatory gene, (h) promoter, (i) transcription factors, and (j) post-transcription process. (sec 25.2) (exercise 25.8, 25.9, 25.10, 2.11, 25.12) 4. Describe ribosomes and discuss their function.(sec 25.3) 5. Show how these relate to each other and how they differ: gene, genetic code, codon and anticodon. (sec 25.3, 25.4) (exercise 25.17, 25.18) 6. Identify
from the structure of a transfer RNA the following: (a) anticodon,
(b) 5’end, (c) 3’ end, and tell (d) where and how (type of chemical bond) the
amino acid bonds to the tRNA. (sec 25.3, 25.5) (exercise
25.15, 25.20) 7. Outline the translation process by which protein synthesis occurs (where these steps take place, how each step starts, proceeds, ends; which enzyme / molecule is involved for what purpose). (sec 25.5) (exercise 25.21, 25.22, 25.23) 8. Use the
genetic code to predict the amino acids sequence in a protein segment given
the sequence of a
segment of mature mRNA. (sec 25.4) 9. Describe
what a mutation is and define the term mutagens. (sec 25.7) 10. Discuss the
different impacts of a mutation and why some are not harmful. (sec 25.7) (exercise
25.29) 11. Explain the
difference between these two terms: recombinant DNA technique and genetic
engineering. (sec 25.8) CHAPTER 31 – BODY FLUIDS
1. Name the
various types of body fluids and point out the special aspects of each type.
(sec 31.1) (exercise 31.2, 31.7, 31.9) 2. Name the
“blood gases” and what it means to “monitor blood gases” in clinical
settings. (lecture notes) 3. Describe the
cell responsible for transporting blood gases, and specify how it is
different from other cells. (sec 31.2) 4. Describe the
general structure of hemoglobin, the number of heme
units in a hemoglobin molecule and the number of oxygen molecules that it can
carry. Determine the oxidation state iron must have in order to bind the O2
molecule.(sec 31.3, sec 21.9, lecture notes) 5. Explain how allosteric interactions affect the affinity of hemoglobin
for oxygen. .(sec 31.3) (exercise 31.13, 31.19) 6. Describe the
three ways carbon dioxide is transported in the blood on the molecular level;
write equations to show carbon dioxide (a) converting into bicarbonate, and
(b) binding to hemoglobin.(sec 31.4) (exercise 31.21) 7. Use the equilibria outlined in page 751 of text and Figure 31.3
to predict how pH of the blood affects the affinity of hemoglobin for oxygen.
(exercise 31.18, 31.22) CHAPTER
26 – BIOENERGETICS: HOW THE BODY CONVERTS FOOD TO ENERGY After completing this chapter, you should
be able to:
1. Compare and
contrast the terms: metabolism, catabolism, and anabolism. (sec 26.1) 2. Define the
phrase: common catabolic pathway. What is its purpose? How does
it relate to the food we eat? (sec 26.1) (exercise 26.2) 3. Describe the
general structure of a cell, in particular describe
in detail the structure of the mitochondrion. (sec 26.2) (exercises
26.3, 26.4, 26.5, 26.6) 4. Give the
full names of the following: ATP, ADP, Acetyl CoA,
FAD, and NAD+. (sec 26.3) (exercise 26.15, 26.18) 5. Write
equations to show the (a) hydrolysis of ATP and (b) the formation of Acetyl CoA when given the structures of ATP and CoA. Explain the role of each process in metabolism. (sec
26.3) (exercise 21.15) 6. Write
equations to show how FAD and NAD+ are reduced. (Note how one gains a hydride
and the other gains a hydride and a proton.) (sec 26.3) (exercise
26.11, 26.12, 26.13, 26.14) 7. Recognize
whether an organic molecule is oxidized or reduced when given the substrate
and the product of a reaction. (lecture notes) 8. Concerning
the citric acid cycle: (Figure 26.8, sec 26.4) (exercises 26.22, 26.24,
26.25, 26.27, 26.28, 26.29) a. List the
general steps: From the 2 carbon fragment of Acetyl CoA
® part of a 6 carbon
molecule (citrate) à 5 carbons à 4 carbons (oxaloacetate), etc. b. Recognize
the names of the intermediates in the citric acid cycle (e.g., citrate, oxaloacetate, etc.); c. If given the
structure of the substrate and product for a specific step in the citric acid
cycle be able to tell what type of reaction it was and whether CO2,
NADH, ATP or FADH2 were produced; d. Tell the
class of enzyme needed to catalyze each step of the citric acid cycle e. Write the
net equation for the citric acid cycle. 9. Concerning
the electron transport chain and oxidative phosphorylation:
(Figure 26.10, sec 26.5, 26.6) (exercises 26.36, 26.38, 26.41, 26.43,
26.44, 26.45) a. Describe in
general the flow of events that take place in the electron transport system. b. Describe in
general what happens in each complex of the electron transport system: which
receive electrons, which pump protons, which are mobile, and where water is
made (including the balanced chemical equation). c. Explain how
coenzyme Q is reduced and how the heme containing cytochromes shuttle electrons. d. Explain what
happens at the ATP synthase complex. What provides
the energy for the reaction? Explain the concept of a proton gradient and
describe how energy can be obtained from it. e. Specify
approximately how many ATP’s are produced from NADH
and FADH2 and use this knowledge to predict how many ATP’s are produced from a given number of acetyl CoA’s through the citric acid cycle and the electron
transport system. 10. Show in
steps how each C2 fragment that enters the citric acid cycle
produces 12 ATP molecules and uses up two O2 molecules. Write an over all
equation for this process (sec 26.7) (exercise
26.50) CHAPTER 27 – SPECIFIC
CATABOLIC PATHWAYS: CARBOHYDRATE, LIPID AND PROTEIN METABOLISM
After completing this chapter you should be able to: 1. Draw an
overall flow chart showing general steps of each specific catabolic pathway
of carbohydrates, proteins and lipids to the common catabolic pathway. (sec
27.1, Figure 27.2) CARBOHYDRATE METABOLISM2. Concerning glycolysis: (sec 27.2) (exercise
27.5, 27.6, 27.7, 27.8, 27.9) a. Describe
what type of reaction occurred if given the substrate and product, b. Given the
substrate, draw the structure of the product in glycolysis
for steps involving keto-enol tautomerization
(isomerization of a aldose to a ketose) or
dehydration. c. Name the 2
major regulatory steps in glycolysis, the steps
that consume or produce ATP, and the step that generates NADH. d. Explain what
substrate level phosphorylation is. e. Explain how
fructose, galactose and mannose enter glycolysis. f.
Write the overall net equation of glycolysis. 3. Discuss the
three possible fate of the pyruvate produced by glycolysis. State the conditions for each fate to occur
and whether NADH is produced or consumed. (lecture notes) (exercise
27.12) 4. Concerning
the pentose phosphate pathway: (sec 27.2, Figure 27.5) (exercise 27.11) a. State the
two main functions of the pentose phosphate pathway. b. Name the two
phases of this pathway. c. State what
each phase of the pathway produces. d. Discuss what
happens if synthesis of nucleic acids is not needed. 5. Show steps
and calculate the number or ATP’s produced from a
molecule of glucose in the presence of oxygen. (sec 27.3)(exercise
27.15, 27.16) 6. Describe how
carbohydrates other than glucose enter the glycolysis
process, including fructose, galactose and the
product of glycogenolysis. (sec 27.3, Figure
27.4)(exercise 27.17) LIPID METABOLISM 7.
Draw structures and write equations to show the
relationship between glycerol, dihydroxyacetone
phosphate and glycerol-3-phosphate. Describe how these molecules relate to
lipid metabolism. (sec 27.4) (exercise 27.19, 27.20) 8. Explain why the catabolism of fatty acids is also called b-oxidation pathway. (sec 27.5) 9. Write an equation to show how a typical fatty acid is activated prior to the beta oxidation. (sec 27.5, Fig 27.6) 10. Specify the part of a cell where each step of fatty acid catabolism occurs, and name the types of chemical reactions involved in each step in the b-oxidation pathway. (sec 27.5, Fig 27.6) (exercise 27.21, 27.22, 27.23) 11. Calculate the number of ATP molecules obtained in the b-oxidation of a typical fatty acid when its formula is given. (sec 27.6)(exercise 27.25, 27.26) 12. Explain the
process of synthesis of ketone bodies (ketogenesis), include the molecules are
they made from, when they are produced, and the names of the three ketone bodies. (sec 27.7) (exercise 27.29, 27.30) PROTEIN AND
AMINO ACID METABOLISM
13. Give an overview
of protein catabolism pathway. (Figure 27.7) 14. Define the
term amino acid pool and list various processes entering and exiting
the amino acid pool. (sec 27.1, Figure 27.7) 15. Predict the
products or give examples of transamination
and oxidative deamination. Describe
where each occurs within the cell and within the organism. (sec 27.8) (exercise
27.33) 16. Describe the Urea cycle in terms of: (sec 27.8) (exercise 27.34, 27.36, 27.37) a. its primary function in the body; b. where it occurs in the body (the point at which the urea cycle moves from the mitochondrial matrix to the cytosol and back to the mitochondrial matrix), c. the reaction for synthesis of carbamoyl phosphate, d. how carbamoyl phosphate enters the urea cycle including the location where this step occurs, e. where each nitrogen and the carbon in urea come from. f. the energy involved in the process, and g. how it relates to the citric acid cycle. 17. Explain why
some amino acids are classified as ketogenic and
others glucogenic and give
two to three examples of each type; discuss the fate of the carbon atoms
belonging to a typical amino acid in each class. (sec 27.9) (exercise
27.35) |