Biochemistry I

Home assignment 1

Student Name:

Fall 2014

Grade: _____/100 points

Assignment date: 09/04/14

Due date: 09/18/14, 9:30 AM
Grading:
a) One point for each correct answer for multiple choice questions. There are 50 multiple
choice questions, so you may earn up to maximum of 50 points.
b) Two points for each correct answer for short answer questions. Do not exceed the space
provided. Be succinct. There are 15 short answer questions, so you may earn up to
maximum of 30 points.
c) Five points for the correct answers to the problem #66.
d) Seven points for identifying the correct sequence of the peptides from the problem #67.
e) Four points for a correct answer for the problem #68.
f) Four points for a correct answer for the problem #69.

Multiple Choice Questions

1. In eukaryotes, the nucleus is enclosed by a double membrane called the:

A)
B)
C)
D)
E)
F)

cell membrane.
nucleolus.
nuclear tire.
nucleoplasm.
nucleosome.
nuclear envelope.

2. The biological classification system categorizes organisms into the domains:

A)
B)
C)
D)
E)

bacteria, eukarya, and vertebrate.

archaea and eukarya.
bacteria, eukarya, and archaea.
eukarya and bacteria.
none of the above

3. The bacterium E. coli requires simple organic molecules for growth and energyit is therefore a:
A)
B)
C)
D)

chemoautotroph.
lithotroph.
lithograph.
chemoheterotroph.

E) photoautotroph.
F) phototraph.
4. The term molecular weight is a term used by biochemists that refers to
A) the density of a particle.
B) a dimensionless quantity that is defined as the ratio of the mass of the particle to 1/12 the mass of
a 12C atom.
C) Daltons divided by the mass of a hydrogen atom.
D) all of the above
E) none of the above
5. Which of the following is not true of eukaryotes:
A)
B)
C)
D)
E)

They contain organelles like mitochondria, chloroplasts, ribosomes, and a nucleus

They are usually 10 to 100 microns in diameter
They can be both uni or multicellular
They are also called archaea
All of the above are true of eukaryotes

6. The three-dimensional structure of macromolecules is formed and maintained primarily through

noncovalent interactions. Which one of the following is not considered a noncovalent interaction?
A)
C)
D)
E)
F)

hydrogen bonds
hydrophobic interactions
ionic interactions
van der Waals interactions
carbon-carbon bonds

7. Stereoisomers that are nonsuperimposable mirror images of each other are known as:
A)
B)
C)
D)
E)

anomers.
cis-trans isomers.
diastereoisomers.
geometric isomers.
enantiomers.

8. The enzyme fumarase catalyzes the reversible hydration of fumaric acid to l-malate, but it will not
catalyze the hydration of maleic acid, the cis isomer of fumaric acid. This is an example of:
A)
B)
C)
D)
E)

biological activity.
stereospecificity.
chiral activity.
racemization.
stereoisomerization.

9. If someone wishes you on your birthday Happy highest entropy to you, this usually means that
he/she wishes you to:

A)
B)
C)
D)
E)
F)

have a dynamic steady state.

have a great activation energy for their enzymes
have a lower metabolism
be disintegrated
have more free energy
none of the above

10. If the free energy change G for a reaction is -46.11 kJ/mol, the reaction is:
A)
B)
C)
D)
E)

at equilibrium.
endergonic.
endothermic.
exergonic.
exothermic.

11. The major carrier of chemical energy in all cells is:

A)
B)
C)
D)
D)
E)

UPS
adenosine monophosphate.
adenosine triphosphate.
FedEx
cytosine tetraphosphate.
uridine diphosphate.

12. The atmosphere of early earth probably contained the following molecules:
A)
B)
C)
D)
E)

H2O, CO2, N2 , CH4, and NH3.

H2O, CO2, CH4, C6H6O6, and NH3.
H2O, CO2, CH4, C6H6O6, and COOHCH2NH3.
H2O, CO2, CH4, COOHCH2NH3, and NH3.
none of the above

13. Which of the following statements about water is incorrect?

A) Water is an excellent solvent for polar molecules
B) Pure water has a concentration of approximately 55.5 M
C) Cations are solvated by shells of water molecules oriented with their hydrogen atoms pointed
toward the ions
D) Non-polar molecules do not dissolve in water, but form a separate phase
E) Amphiphilic detergents often form micelles with the polar groups on the outside exposed to the
water (solvent) and the non-polar groups sequestered in the interior
14. The pH of a sample of blood is 7.4, while gastric juice is pH 1.4. The blood sample has:
A)
B)
C)
D)
E)

5.29 times lower [H+] than the gastric juice.

6 times lower [H+] than the gastric juice.
6,000 times lower [H+] than the gastric juice.
a million times lower [H+] than the gastric juice.
0.189 times the [H+] as the gastric juice.

15. Phosphoric acid is tribasic, with pKas of 2.14, 6.86, and 12.4. The ionic form that predominates at
pH 3.2 is:
A)
B)
C)
D)
E)

H3PO4.
HPO42.
PO43.
H2PO4.
None of the above.

16. Which of the following statements about buffers is true?

A)
B)
C)
D)
E)

A buffer composed of a weak acid of pKa = 5 is stronger at pH 4 than at pH 6.

At pH values lower than the pKa, the salt concentration is higher than that of the acid.
The strongest buffers are those composed of strong acids and strong bases.
When pH = pKa, the weak acid and salt concentrations in a buffer are equal.
The pH of a buffered solution remains constant no matter how much acid or base is added to the
solution.

17. The Henderson-Hasselbalch equation:

A)
B)
C)
D)
E)

allows the graphic determination of the molecular weight of a weak acid from its pH alone.
does not explain the behavior of di- or tri-basic weak acids
employs the same value for pKa for all weak acids.
relates the pH of a solution to the pKa and the concentrations of acid and conjugate base.
is equally useful with solutions of acetic acid and of hydrochloric acid.

18. Consider an acetate buffer, initially at the same pH as its pKa (4.76). When sodium hydroxide
(NaOH) is mixed with this buffer, the:
A)
B)
C)
D)
E)

pH remains constant.
pH rises more than if an equal amount of NaOH is added to an acetate buffer initially at pH 6.76.
pH rises more than if an equal amount of NaOH is added to unbuffered water at pH 4.76.
sodium acetate formed precipitates because it is less soluble than acetic acid.
ratio of acetic acid to sodium acetate in the buffer falls.

19. The chirality of an amino acid results from the fact that its carbon:
A)
B)
C)
D)
E)

has no net charge.

is bonded to four different chemical groups.
is a carboxylic acid.
is in the L absolute configuration in naturally occurring proteins.
is symmetric.

20. Of the 20 standard amino acids, only ___________ is not optically active. The reason is that its
side chain ___________.
A)
B)
C)
D)

alanine; is a simple methyl group

glycine; is a hydrogen atom
glycine; is unbranched
lysine; contains only nitrogen

E) proline; forms a covalent bond with the amino group

21. Which of the following statements about aromatic amino acids is correct?
A) All are strongly hydrophilic.
B) Histidines ring structure results in its being categorized as aromatic or basic, depending on pH.
C) The major contribution to the characteristic absorption of light at 280 nm by proteins is the
phenylalanine R group.
D) On a molar basis, tryptophan absorbs more ultraviolet light than tyrosine.
E) The presence of a ring structure in its R group determines whether or not an amino acid is
aromatic.
22. Which of the following statements about cystine is correct?
A) Cystine is an example of a nonstandard amino acid, derived by linking two standard amino acids.
B) Cystine is formed by the oxidation of the carboxylic acid group on cysteine.
C) Cystine forms when the CH2SH R group is oxidized to form a CH2SSCH2
disulfide bridge between two cysteines.
D) Cystine is formed through a peptide linkage between two cysteines.
E) Two cystines are released when a CH2SSCH2 disulfide bridge is reduced to CH2
SH.
23. The uncommon amino acid selenocysteine has an R group with the structure CH2SeH (pKa
5). In an aqueous solution, pH = 7.0, selenocysteine would:
A)
B)
C)
D)
E)

be found in proteins as D-selenocysteine.

never be found in a protein.
be nonionic.
be a fully ionized zwitterion with no net charge.
not be optically active.

24. For amino acids with neutral R groups, at any pH below the pI of the amino acid, the population of
amino acids in solution will have:
A)
B)
C)
D)
E)

a net negative charge.

a net positive charge.
no charged groups.
no net charge.
positive and negative charges in equal concentration.

25. At pH 7.0, converting a proline to hydroxyproline will have what effect on the overall charge of the
protein containing it?
A)
B)
C)
D)
E)

It will become more negative

It will become more positive.
There is not enough information to answer the question.
It will stay the same.
the answer depends on the salt concentration.

26. At pH 7.0, converting a glutamic acid to -carboxyglutamate will have what effect on the overall
charge of the protein containing it?

A)
B)
C)
D)
E)

It will become more negative

It will become more positive.
It will stay the same.
There is not enough information to answer the question.
The answer depends on the salt concentration.

27. Which of the following tripeptides would be expected to be the most hydrophobic:
A)
B)
C)
D)
E)

KYG
KYA
GYA
DYA
DYG

28. At pH 7, arginine (pKs are alpha-carboxylate 1.82, alpha-amino 8.99, guanidino 12.48) would be
charged as follows:
A)
B)
C)
D)
E)

0 alpha-carboxylate, 0 alpha-amino, +1 guanidino, +1 net charge

+1 alpha-carboxylate, 0 alpha-amino, -1 guanidino, 0 net charge
+1 alpha-carboxylate, -1 alpha-amino, -1 guanidino, -1 net charge
-1 alpha-carboxylate, +1 alpha-amino, +1 guanidino, +1 net charge
-1 alpha-carboxylate, 0 alpha-amino, +1 guanidino, 0 net charge

29. At pH 7, aspartic acid (pKs are alpha-carboxylate 1.99, alpha-amino 9.9, beta-carboxylate 3.9 )
would be charged as follows:
A)
B)
C)
D)
E)

0 alpha-carboxylate, +1 alpha-amino, 0 beta-carboxylate, +1 net charge

-1 alpha-carboxylate, +1 alpha-amino, -1 beta-carboxylate, -1 net charge
0 alpha-carboxylate, -1 alpha-amino, 0 beta-carboxylate, -1 net charge
+1 alpha-carboxylate, -1 alpha-amino, +1 beta-carboxylate, +1 net charge
+1 alpha-carboxylate, +1 alpha-amino, +1 beta-carboxylate, +3 net charge

30. At pH 11, glutamic acid (pKs are alpha-carboxylate 2.1, alpha-amino 9.47, gamma-carboxylate
4.07. would be charged as follows:
A)
B)
C)
D)
E)

+1 alpha-carboxylate, 0 alpha-amino, +1 gamma-carboxylate, +2 net charge

-1 alpha-carboxylate, +1 alpha-amino, -1 gamma-carboxylate, -1 net charge
0 alpha-carboxylate, 0 alpha-amino, 0 gamma-carboxylate, 0 net charge
+1 alpha-carboxylate, -1 alpha-amino, +1 gamma-carboxylate, +1 net charge
-1 alpha-carboxylate, 0 alpha-amino, -1 gamma-carboxylate, -2 net charge

31. At pH 4, histidine (pKs are alpha-carboxylate 1.8, alpha-amino 9.33, 6.04 imidazole) would be
charged as follows:
A)
B)
C)
D)

+1 alpha-carboxylate, 0 alpha-amino, -1 imidazole, 0 net charge

-1 alpha-carboxylate, +1 alpha-amino, 0 imidazole, 0 net charge
+1 alpha-carboxylate, +1 alpha-amino, -1 imidazole, +1 net charge
-1 alpha-carboxylate, +1 alpha-amino, +1 imidazole, +1 net charge

E) 0 alpha-carboxylate, + alpha-amino, +1 imidazole, +2 net charge

32. At pH 5, cysteine (pKs are alpha-carboxylate 1.92, alpha-amino 10.7, sulfhydryl 8.37 ) would be
charged as follows:
A)
B)
C)
D)
E)

0 alpha-carboxylate, 0 alpha-amino, 0 sulfhydryl, 0 net charge

+1 alpha-carboxylate, -1 alpha-amino, -1 sulfhydryl, -1 net charge
-1 alpha-carboxylate, +1 alpha-amino, +1 sulfhydryl, +1 net charge
-1 alpha-carboxylate, +1 alpha-amino, 0 sulfhydryl, 0 net charge
+1 alpha-carboxylate, -1 alpha-amino, 0 sulfhydryl, 0 net charge

33. At pH 1, lysine (pKs are alpha-carboxylate 2.16, alpha-amino 9.06, epsilon-amino 10.54 ) would be
charged as follows:
A)
B)
C)
D)
E)

0 alpha-carboxylate, -1 alpha-amino, -1 epsilon-amino, -2 net charge

-1 alpha-carboxylate, +1 alpha-amino, +1 epsilon-amino, +1 net charge
+1 alpha-carboxylate, +2 alpha-amino, +2 epsilon-amino, +5 net charge
0 alpha-carboxylate, +1 alpha-amino, +1 epsilon-amino, +2 net charge
+2 alpha-carboxylate, +1 alpha-amino, +1 epsilon-amino, +4 net charge

34. Amino acid side-chain residues have:

A)
B)
C)
D)
E)

a positive charge in every situation

pKs that assure the solubility of every protein
constant pKs no matter what aqueous environment they are found in
different pKs in peptides as compared to the free amino acids
polar functional groups

35. The formation of a peptide bond between two amino acids is an example of a(n) ______________
reaction.
A)
B)
C)
D)
E)

cleavage
condensation
group transfer
isomerization
oxidation reduction

36. At the isoelectric pH of a tetrapeptide:

A)
B)
C)
D)
E)

only the amino and carboxyl termini contribute charge.

the amino and carboxyl termini are not charged.
the total net charge is zero.
there are four ionic charges.
two internal amino acids of the tetrapeptide cannot have ionizable R groups.

37. The average molecular weight of the 20 standard amino acids is 138, but biochemists use 110 when
estimating the number of amino acids in a protein of known molecular weight. Why?
A) The number 110 is based on the fact that the average molecular weight of a protein is 110,000
with an average of 1,000 amino acids.
B) The number 110 reflects the higher proportion of small amino acids in proteins, as well as the

loss of water when the peptide bond forms.

C) The number 110 reflects the number of amino acids found in the typical small protein, and only
small proteins have their molecular weight estimated this way.
D) The number 110 takes into account the relatively small size of nonstandard amino acids.
E) The number 138 represents the molecular weight of conjugated amino acids.
38. For the study of a protein in detail, an effort is usually made to first:
A)
B)
C)
D)
E)

conjugate the protein to a known molecule.

determine its amino acid composition.
determine its amino acid sequence.
determine its molecular weight.
purify the protein.

39. In a mixture of the five proteins listed below, which should elute second in size-exclusion (gelfiltration) chromatography?
E)
A)
B)
C)
D)

serum albumin
cytochrome c
immunoglobulin G
ribonuclease A
RNA polymerase

Mr = 68,500
Mr = 13,000
Mr = 145,000
Mr = 13,700
Mr = 450,000

40. The following reagents are often used in protein chemistry. Match the reagent with the purpose for
which it is best suited. Some answers may be used more than once or not at all; more than one
reagent may be suitable for a given purpose.
(a) CNBr (cyanogen bromide)
(b) Edman reagent (phenylisothiocyanate)
(c) FDNB
(d) dithiothreitol

(e) performic acid

(f) chymotrypsin
(g) trypsin

___ hydrolysis of peptide bonds on the carboxyl side of Lys and Arg
___ cleavage of peptide bonds on the carboxyl side of Met
___ breakage of disulfide (SS) bonds
___ determination of the amino acid sequence of a peptide
___ determining the amino-terminal amino acid in a polypeptide
41. By adding SDS (sodium dodecyl sulfate) during the electrophoresis of proteins, it is possible to:
A)
B)
C)
D)
E)

determine a proteins isoelectric point.

determine an enzymes specific activity.
determine the amino acid composition of the protein.
preserve a proteins native structure and biological activity.
separate proteins exclusively on the basis of molecular weight.

42. The first step in two-dimensional gel electrophoresis generates a series of protein bands by
isoelectric focusing. In a second step, a strip of this gel is turned 90 degrees, placed on another gel
containing SDS, and electric current is again applied. In this second step:
A) proteins with similar isoelectric points become further separated according to their molecular

weights.
B) the individual bands become stained so that the isoelectric focus pattern can be visualized.
C) the individual bands become visualized by interacting with protein-specific antibodies in the
second gel.
D) the individual bands undergo a second, more intense isoelectric focusing.
E) the proteins in the bands separate more completely because the second electric current is in the
opposite polarity to the first current.
43. One method used to prevent disulfide bond interference with protein sequencing procedures is:
A) cleaving proteins with proteases that specifically recognize disulfide bonds.
B) protecting the disulfide bridge against spontaneous reduction to cysteinyl sulfhydryl groups.
C) reducing disulfide bridges and preventing their re-formation by further modifying the SH
groups.
D) removing cystines from protein sequences by proteolytic cleavage.
E) sequencing proteins that do not contain cysteinyl residues.
44. Which one of the tripeptides below:
A
B
C
D
E
__________________________________________________________________
Tyr-Lys-Met Gly-Pro-Arg
Asp-Trp-Tyr
Asp-His-Glu
Leu-Val-Phe
____(a) is most negatively charged at pH 7?
____(b) will yield DNP-tyrosine when reacted with l-fluoro-2,4-dinitrobenzene and
hydrolyzed in acid?
____(c) contains the largest number of nonpolar R groups?
____(d) contains sulfur?
____(e) will have the greatest light absorbance at 280 nm?
45. A nonapeptide was determined to have the following amino acid composition: (Lys)2, (Gly) 2, (Phe)
2, His, Leu, Met. The native peptide was incubated with 1-fluoro-2,4-dinitrobenzene (FDNB) and
then hydrolyzed; 2,4-dinitrophenylhistidine was identified by HPLC. When the native peptide was
exposed to cyanogen bromide (CNBr), an octapeptide and free glycine were recovered. Incubation
of the native peptide with trypsin gave a pentapeptide, a tripeptide, and free Lys. 2,4Dinitrophenyl-histidine was recovered from the pentapeptide, and 2,4-dinitrophenylphenylalanine
was recovered from the tripeptide. Digestion with the enzyme pepsin produced a dipeptide, a
tripeptide, and a tetrapeptide. The tetrapeptide was composed of (Lys) 2, Phe, and Gly. The native
sequence was determined to be:
A)
B)
C)
D)
E)

GlyPheLysLysGlyLeuMetPheHis.
HisLeuGlyLysLysPhePheGlyMet.
HisLeuPheGlyLysLysPheMetGly.
HisPheLeuGlyLysLysPheMetGly.
MetLeuPheLysPheGlyGlyLysHis.

46. In the diagram below, the plane drawn behind the peptide bond indicates the:

A)
B)
C)
D)
E)

absence of rotation around the CN bond because of its partial double-bond character.
plane of rotation around the CN bond.
region of steric hindrance determined by the large C=O group.
region of the peptide bond that contributes to a Ramachandran plot.
theoretical space between 180 and +180 degrees that can be occupied by the and angles in
the peptide bond.

47. The -keratin chains indicated by the diagram below have undergone one chemical step. To alter
the shape of the -keratin chainsas in hair wavingwhat subsequent steps are required?

A)
B)
C)
D)
E)

Chemical oxidation and then shape remodeling

Chemical reduction and then chemical oxidation
Chemical reduction and then shape remodeling
Shape remodeling and then chemical oxidation
Shape remodeling and then chemical reduction

48. Which of the following statements about oligomeric proteins is false?

A)
B)
C)
D)
E)

A subunit may be similar to other proteins.

All subunits must be identical.
Many have regulatory roles.
Some oligomeric proteins can further associate into large fibers.
Some subunits may have nonprotein prosthetic groups.

49. An average protein will not be denatured by:

A)
B)
C)
D)
E)

a detergent such as sodium dodecyl sulfate.

heating to 90C.
iodoacetic acid.
pH 10.
urea.

50. Experiments on denaturation and renaturation after the reduction and reoxidation of the SS
bonds in the enzyme ribonuclease (RNase) have shown that:
A) folding of denatured RNase into the native, active conformation requires the input of energy in
the form of heat.
B) native ribonuclease does not have a unique secondary and tertiary structure.
C) the completely unfolded enzyme, with all SS bonds broken, is still enzymatically active.
D) the enzyme, dissolved in water, is thermodynamically stable relative to the mixture of amino
acids whose residues are contained in RNase.
E) the primary sequence of RNase is sufficient to determine its specific secondary and tertiary
structure.

Short Answer Questions

51. Why is an asymmetric carbon atom called a chiral center?

52. Differentiate between configuration and conformation.

53. (a)Briefly define isotonic, hypotonic, and hypertonic solutions. (b) Describe what happens
when a cell is placed in each of these types of solutions.

54. Give the general Henderson-Hasselbalch equation and sketch the plot it describes (pH against
amount of NaOH added to a weak acid). On your curve label the pKa for the weak acid, and
indicate the region in which the buffering capacity of the system is greatest.

55. Leucine has two dissociable protons, one with a pKa of 2.3, the other with a pKa of 9.7. Sketch a
properly labeled titration curve for leucine titrated with NaOH; indicate where the pH = pK and the
region(s) in which buffering occurs.

56. Draw the structure of a) Arginine, b) Glutamate, 3) Tyrosine and 4) +H3N-Arg-Glu-Tyr-COO- in

zwiterionic form and their ionized forms at low pH, neutral pH and high pH

57. For each of these methods of separating proteins, describe the principle of the method, and tell what
property of proteins allows their separation by this technique.
(a) ion-exchange chromatography
(b) size-exclusion (gel filtration) chromatography
(c) affinity chromatography

58. A biochemist is attempting to separate a DNA-binding protein (protein X) from other proteins in a
solution. Only three other proteins (A, B, and C) are present. The proteins have the following
properties:
pI
(isoelectric
Size
Bind to
point)
Mr
DNA?

protein A
7.4
82,000
yes
protein B
3.8
21,500
yes
protein C
7.9
23,000
no
protein X
7.8
22,000
yes

What type of protein separation techniques might she use to separate

(a) protein X from protein A?
(b) protein X from protein B?
(c) protein X from protein C?

59. How can isoelectric focusing be used in conjunction with SDS gel electrophoresis?

60. In one or two sentences, describe the usefulness of each of the following reagents or reactions in the
analysis of protein structure:
(a) Edman reagent (phenylisothiocyanate)
(b) Sanger reagent (1-fluoro-2,4-dinitrobenzene, FDNB)
(c) trypsin

61. A biochemist wishes to determine the sequence of a protein that contains 123 amino acid residues.
After breaking all of the disulfide bonds, the protein is treated with cyanogen bromide (CNBr), and
it is determined that that this treatment breaks up the protein into seven conveniently sized peptides,
which are separated from each other. It is your turn to take over. Outline the steps you would take
to determine, unambiguously, the sequence of amino acid residues in the original protein.

62. You are trying to determine the sequence of a protein that you know is pure. Give the most likely
explanation for each of the following experimental observations. You may use a simple diagram
for your answer.
(a) The Sanger reagent (FDNB, fluorodinitrobenzene) identifies Ala and Leu as aminoterminal residues, in roughly equal amounts.
(b) Your protein has an apparent Mr of 80,000, as determined by SDS-polyacrylamide gel
electrophoresis. After treatment of the protein with performic acid, the same technique
reveals two proteins of Mr 35,000 and 45,000.
(c) Size-exclusion chromatography (gel filtration) experiments indicate the native protein has
an apparent Mr of 160,000.

63. Describe two major differences between chemical synthesis of polypeptides and synthesis of
polypeptides in the living cell.

64. Explain how circular dichroism spectroscopy could be used to measure the denaturation of a
protein.

65. Each of the following reagents or conditions will denature a protein. For each, describe in one or
two sentences what the reagent/condition does to destroy native protein structure.
(a)
(b)
(c)
(d)

urea
high temperature
detergent
low pH

66. Problem:
In one of the attached ppt there are two ESI-MS spectra of two proteins. Determine charge state of
two adjacent peaks from each spectrum and use them to identify the mass of each protein.

67. Problem: The attached ppt represents the MS/MS spectrum of a synthetic peptide. Determine the
sequence of this peptide using de novo sequencing, described in the attached pdf material. The
theoretical m/z of the precursor is [MH]+ = 1570.67 (monoisotopic) and [MH]2= 785.84.

Slide 1 shows the full MS/MS spectrum of the precursor, observed as m/z of [MH]2+ as 785.85.
Peaks 1384.61 and 1441.63 have low intensity, but are shown because they are important for
determining the peptide sequence. Slides 2 and 3 show the enhanced MSMS spectrum already shown
in slide 1. Slide 4 shows the precursor ion.
After you determined the sequence of the peptide, look at slide 5 and try to explain the pairs of peaks
that appear at 942.58 and 924.55, 1056.60 and 1039.56, 1171.61 and 1154.68, and 1285.65 and
1268.69, just by looking at the sequence of the peptide and at the intrinsic properties of particular
amino acids. Do the same for the pair of peaks from slide 6.

68. Problem: Describe a purification procedure for a mitochondrial (membrane or soluble) protein from
either plant or animal source.

69. Draw the structure of the 20 amino acids