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2. Which of these elements is the least common in organic compounds within living cells?
a)
b)
c)
d)
e)
carbon
hydrogen
nitrogen
sulfur
fluoride
3. If the hydrogen ion concentration of the blood increases ten-fold, how much does the pH
change?
a)
b)
c)
d)
e)
4. If the pH changes from 7.0 to 6.0 which amino acid R-group is the most affected?
(Hint: The most affected R-group is the one with a pK the closest to pH 7.0)
a)
b)
c)
d)
e)
arginine
glutamate
lysine
aspartate
histidine
5. Which type of bond involves shared electrons and serves as the basic linkage in organic
compounds?
a)
b)
c)
d)
e)
ionic
hydrogen
hydrophobic
covalent
van der Waals forces
6. Which amino acid is essentially incompatible with alpha helix and beta sheet formation?
a)
b)
c)
d)
e)
histidine
tryptophan
alanine
proline
cysteine
8. In proteins the R-groups of the polar but uncharged amino acids, serine and glutamine
generally can form _______ bonds with each other.
a)
b)
c)
d)
e)
Hydrogen
Hydrophobic
Ionic
Peptide
Disulfide
9. The side chains of valine and isoleucine can form _______ bonds with each other.
a)
b)
c)
d)
e)
Hydrogen
Hydrophobic
Ionic
Peptide
Disulfide
10. Which amino acid changes the charge on its R-group as a function of pH?
a)
b)
c)
d)
e)
Lysine
Leucine
Isoleucine
Valine
Methionine
weak acids
weak bases
strong acids
strong bases
none of the above
13. Which of the following does NOT contain a type of amide bond?
a.
b.
c.
d.
e.
14. A purification method which depend on highly selective interactions between a proteins
binding site and a specific ligand ________.
a)
b)
c)
d)
e)
16. What type of protein would stick very tightly to a positively charged DEAE-cellulose ion
exchange column?
a)
b)
c)
d)
e)
18. A technique that is used to determine the three dimensional form of a protein is:
a)
b)
c)
d)
e)
NMR
Gel filtration
Mass Spectrometry
Ion exchange chromatography
X-ray Diffraction
21. What is the primary reagent used to sequence proteins during the Edman degradation?
a)
b)
c)
d)
e)
ninhydrin
trypsin.
pepsin
phenylisothiocyanate
chymotrypsin
22. What reagent is used to prevent reoxidation of sulfhydryl groups during the reduction of
protein disulfides:
a)
b)
c)
d)
e)
hydrochloric acid
iodoacetate
succinate
cyanogen bromide
cesium chloride
23. The phi and psi bonds that flank peptide bonds in proteins:
a)
b)
c)
d)
e)
rotate freely and can assume almost any combination of bond angles
are able to rotate but generally assume certain combinations of bond angles
do not rotate at all because they are planar
only rotate in a few selective locations in the protein
are compatible with alpha helix but not with beta sheet sturctures
24. The overall free energy change for a chemical reaction is positive if the reaction:
a)
b)
c)
d)
e)
27. Biochemists use a modified form of the standard free energy because:
a)
b)
c)
d)
e)
28. The factor which measures the number of molecules of substrate reacted per enzyme
active site and which does not change as an enzyme is purified:
a)
b)
c)
d)
e)
Vmax
Km
Turnover number
Specific activity
Keq
29. Which of the following is NOT true about the ATP cofactor:
a)
b)
c)
d)
e)
vary in rate but ultimately can produce the same level of product
have the same energy of activation
have the same reaction pathway
have different standard free energy values
have different equilibrium constants
32. Which of the following is NOT true about the 20 common amino acids:
a)
b)
c)
d)
e)
33. What are the four levels of protein structure and what kinds of bonds contribute to and
stabilize each level of structure?
.
34. Outline the various ways in which enzyme reactions differ from analogous chemical
reactions.
35. How and why are protein molecules affected by the pH of the environment? How can the
Henderson-Hasselbalch equation be used to tell us about the response of protein
molecules to changes in pH?
36. Describe the use of affinity chromatography and explain why it is such a powerful
technique for purifying proteins. Why is it more powerful than most other methods?