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BCHS > exam 2 (lec. 7-12) > Flashcards

exam 2 (lec. 7-12) Flashcards

1
Q

How many methods are commonly used in protein purification?

A. 0
B. 1
C. 2
D. 3

A

D. 3

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2
Q

I have a dimer of 20 kDa protein. What size permeable membrane should I use?
A. 10 kDa
B. 15 kDa
C. 30 kDa
D. 50 kDa

A

B. 15 kDa

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3
Q

Which is NOT an affinity purification type residue?

A. Antibody
B. Cationic
C. DNA
D. Ligand

A

B. Cationic

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4
Q

What do larger spots represent in 2D gels?

A

Larger Proteins

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5
Q

The primary sequence of protein is the:

A. Amino Acid code
B. Helices and sheets
C. Protein structure
D. Protein Complex

A

Amino Acid code

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6
Q

Two enzymes were used to cleave the fragment and the pieces generated were TS, ACGTY, and KANRVW or ANR, VTWS, and ACGTYK. What is the starting fragment?

A. ACGTYKVWTSPNR
B. ACGTYKANRVWTS
C. KANRVWACGTYTS
D. TSACGTYKANRVW

A

B. ACGTYKANRVWTS

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7
Q

Which amino acid is the least common:

A. Met
B. Phe
C. Ser
D. Val

A

A. Met

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8
Q

Which proteases were used to generate the previous fragments?

A. Chymotrypsin and Pepsin
B. Thermolysin and Pepsin
C. Trypsin and Chymotrypsin
D. Trypsin and Endopeptidase V8

A

C. Trypsin and Chymotrypsin

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9
Q

Can you cleave a protein with trypsin and identify the protein if previously known?

A. True
B. False

A

A. True

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10
Q

Given the genetic code and the number of known proteins, how many amino acids must you sequence from the N-terminal to identify a protein?

A. 1
B. 10
C. 100
D. The whole protein

A

B. 10

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11
Q

An anion exchange resin purifies a protein based largely on:

A. Hydrophobicity
B. Negative Charge
C. Positive Charge
D. Size

A

B. Negative Charge

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12
Q

Given the following trypsin fragments YR, QMK, FAMK, and GMDIK and the CNBR fragments of K, KFAM, YRGM, and DIKQM, what is the starting fragment?

A. FAMKQMKYRGMDIK
B. KFAMYRGMDKQMK
C. GMDIKFAMKYRQMK
D. YRGMDIKQMKFAMK

A

D. YRGMDIKQMKFAMK

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13
Q

The sickle cell mutation is an example of what type of protein mutation:

A. Conserved
B. Non-conserved
C. Silent mutatino
D. Cannot tell

A

B. Non-Conserved

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14
Q

Which PAM score is more closely related?

A. 5
B. 25
C. 40
D. 50

A

5

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15
Q

Do genes which have been duplicated have the same general function?
The same role in the organism?

A. No and No
B. No and Yes
C. Yes and No
D. Yes and Yes

A

C. Yes and No

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16
Q

The homologous A and B domain of the catalytic subunit likely occurred because of:

A

GENE DUPLICATION

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17
Q

All the proteins represented come from mammals.
A. True
B. False

A

B. False

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18
Q

In the previous graph, the further away the vertical line is from the protein the:
A. more related the protein is
B. the more unrelated the protein is
C. does not say anything about relatedness
D. the more homology a protein has

A

B. the more unrelated the protein is

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19
Q

The more complete the grey line is the more ___ an amino acid is.

A. conserved
B. hydrophobic
C. Acidic
D. structurally important

A

A. Conserved

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20
Q

The Ramachandran plot shows what of protein?

A

Structure/Angles/Steric Hindrance

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21
Q

Protein alpha helices by and large are:

A. composed of prolines
B. left-handed
C. right-handed
D. all have consistent distances between AA’s

A

C. Right-handed

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22
Q

Beta sheets

a. have a distance of 7 angstroms between residues
b. can be parallel or anti paralle
c. amino acid sidechains alternate location
d. all of the above statements are true

A

d. all of the above statements are true

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23
Q

Loops in proteins are:
a. the least mutated areas
b. always rigid
c. flexible
d. never random coils

A

c. Flexible

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24
Q

Given the Chou-Fasman chart, Tyr is most likely to be:

a. found in alpha helix
b. found in a beta sheet
c. both structures about equally
d. not enough information

A

b. Found in a beta sheet

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25
Q

Given the Chou-Fasman chart, the sequence EIMALQDP is most likely a(n):
a. alpha helix
b. beta sheet
c. random coil
d. cannot tell

A

a. Alpha helix

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26
Q

The amino acids (EIMALQDP) would likely be found in which region of the plot:
a. 1
b. 2
c. 3
d. 4

A

b. 2

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27
Q

What amino acid would likely be found in region 4?

a. Gly
b. Glu
C. Pro
D. Tyr

A

A. Gly

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28
Q

Where is keratin structure NOT found?

A. Bone
B. Feather
C. Hair
D. Nails

A

A. Bone

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29
Q

Which amino acid is NOT part of silk?

A. Ala
B. Gly
C. Phe
D. Ser

A

C. Phe

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30
Q

Which modified amino acid is found in collagen?

A. Gly
B. Glu
C. Pro
D. Phe

A

C. Pro

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31
Q

Which vitamin is necessary for modification of proline?
A. Vitamin A
B. Vitamin B
C. Vitamin C
D. Vitamin D

A

C. Vitamin C

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32
Q

Which group does the following amino acid, Aspartic Acid, belong to?

A

Polar

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33
Q

Which structural protein is found as beta sheet?

A. Collagen
B. Keratin
C. Silk
D. None of the above

A

C. Silk

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34
Q

For amino acids with neutral (non-ionizing) R groups, at any pH below the pI of the the amino acid, the population of amino acids in solution will:

A

have a net POSITIVE charge

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35
Q

What is the primary function of SDS in SDS-PAGE?

A. to visualize proteins under UV
B. To denature proteins and impart a negative charge
C. To impart a uniform positive charge
D. None of the above
E. To provide conducitivity for the gel

A

B. To denature proteins and impart a negative charge

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36
Q

Given pK1 = 2.35 and pK2 = 9.87, select its correct charge at pH 13.

A

-1

pH > pka’s

if pH<pka’s, +1
if pk1<pH<pk2, 0
pH = pk1, 1/2
pH = pk2, -1/2

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37
Q

Two dimensional electrophoresis is a combination of which two techniques?

A. Ion-exchange chromatography and SDS-Page
B. Isoelectric focusing and affinity chromatography
C. Isoelectric focusing and ion-exchange chromatography
D. Affinity and SDS-PAGE
E. Isoelectric focusing and SDS-Page

A

E. Isoelectric focusing and SDS-PAGE

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38
Q

Most proteins are purified using characteristics such as:
A. Size
B. Solubility
C. Charge
D. Specific binding affinity
E. All of the above

A

E. All of the above

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39
Q

The secondary structure of a protein is primarily maintained by:
A. Hydrogen bonds
B. All of the above
C. Van der Waals
D. Hydrophobic bonds
E. Ionic Bonds

A

A. Hydrogen Bonds

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40
Q

The backbone of a protein has an alternating ____ sequence.

A

C-C-N

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41
Q

In what order would the amino acids Arg, His, and Leu be eluted from a carboxymethyl column at pH 6?

A

Leu, His, Arg

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42
Q

In what order would Glu, Lys, and Val be eluted from a diethyl aminoethyl (positively charged resin) column at pH8?

A

Lys, Val, Glu
KVE

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43
Q

The quaternary structure of hemoglobin has how many peptides?

a. 1
b. 2
c. 3
d. 4

A

d. 4
2 alpha and 2 beta subunits

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44
Q

In order to follow the purity of an enzyme, you need:
a. a method to measure the activity
b. an antibody against the enzyme
c. to be able to run SDS/Page
d. None of the above

A

a. a method to measure the activity

45
Q

Which type of protein purification is, generally, the most expensive
a. affinity purification
b. ion exchange
c. phase separation
d. size exclusion

A

Affinity purification

46
Q

The primary sequence of a protein is
a. the local special alignment of amino acids without regards to side chains
b. the linear sequence of amino acids
c. the 3-dimensional structure of the peptide
c. 2 or more peptide chains associated with a protein

A

The linear sequence of amino acids (AA code)

47
Q

In order to purify a protein, you:

a. must use an affinity column
b. must protect against denaturation of the protein
c. must allow cleavage of the protein by proteases
d. all of the above

A

b.must protect against denaturation of the protein

48
Q

For protein isolation, you need:

a. a good source of protein
b. a sensitive detection method
c. both the above
d. neither the above

A

c. both the above

49
Q

Which is a strategy of purification?

a. charge
b. polarity
c. solubility
d. all of the above

A

d. all of the above

50
Q

Which is NOT a type of chromatography?

a. liquid
b. gas
c. solid state
d. affinity

A

c. Solid State

51
Q

The first protein sequenced was

a. myoglobin
b. hemoglobin
c. insulin
d. beta galactosidase

A

c. INSULIN

think pig OINK!

52
Q

What is the max. number of amino acids that can be sequenced using Edman degradation?

a. 25
b. 50
c. 75
d. 100

A

b. 50!

Mr.Edmand is 50 yrs old

53
Q

Which is the least common amino acid in proteins?

a. Ala
b. Gly
c. Glu
d. Trp

A

d. TRP!

tripping is unlikely in sneakers

54
Q

Which enzyme will cleave near a Tyr residue?

a. chymotrypsin
b. endopeptidase v8
c. thermolysin
d. trypsin

A

Chymotrypsin

Residues that chymotrypsin cleaves: Phe, Trp, Tyr

55
Q

In sickle cell anemia, the normal hemoglobin’s amino acid of Glu is mutated to ___

a. Asp
b. Cys
c. Phe
d. Val

A

Val

56
Q

Sickle cell anemia serves a protective role against malaria which normally occurs in:
a. Congo
b. England
c. Germany
d. South Africa

A

a. Congo

57
Q

Which drink was historically used to combat malaria?
a. beer
b. gin and tonic
c. jack daniels and coke
d. tequila and lime

A

Gin and tonic

58
Q

Myoglobin’s main role is to:
a. cleave proteins
b. generate ATP
c. store oxygen
d. transport oxygen throughout the body

A

Store oxygen

59
Q

DNA mutation rates are:
a. constant
b. dependent on the organism’s lifespan
c. depend on the size of the genome
d. random

A

a. constant

60
Q

Protein families are:
a. composed of homologous proteins
b. have mutations to key structural amino acids
c. not related evolutionarily
d. show mutations to enzymatically important residues

A

a. composed of homologous proteins

61
Q

In a phylogenetic tree, each branch represents:
a. common ancestors
b. conservative mutations
c. non conservative mutations
d. related proteins

A

a. common ancestors

62
Q

Which is a conservative mutation?
a. Ala to Phe
b. Glu to Asp
c. Leu to Lys
d. Thr to Trp

A

b. Glu to Asp

63
Q

Evolution through gene duplication:
a. produce related proteins
b. once duplicated, individual genes can mutate into separate genes
c. result in proteins which evolve with different properties
d. all of the above

A

d. all of the above

64
Q

Protein mutation rates:
a. are constant
b. differ bc of varying rates of DNA mutations
c. differ bc of differing RNA mutation rates
d. vary due to mutations to necessary amino acids

A

d. vary due to mutations to necessary amino acids

65
Q

Which region of the Ramachandran plot is indicative of a beta sheet?
a. 1
b. 2
c. 3
d. 4

A

a. 1

66
Q

An alpha helix has how many amino acids per turn?
a. 2.2
b. 3
c. 3.6
d. 4

A

c. 3.6

67
Q

A left-handed helix is compromised mostly of:
a. Ala
b. Phe
c. Pro
d. Thr

A

Pro

Pro/left = liberal

68
Q

In the NM nomenclature for helices, the M stands for:
a. the # of amino acids in a turn
b. the pitch of the helix
c. The number of atoms that complete the cyclic system that is enclosed by the hydrogen bond
d. none of the above

A

c. The number of atoms that complete the cyclic system that is enclosed by the hydrogen bond

69
Q

The repeat distance in beta sheets is __ angstroms
a. 2
b. 3.5
c. 7
d. 10

A

c. 7

70
Q

An anti-parallel beta sheet ___ stable than a parallel beta sheet
a. has the same stability as
b. is equally as
c. is less
d. is more

A

d. is more

71
Q

Which is composed of triple left-handed helices forming a right-handed coil?
a. collagen
b. keratin
c. hemoglobin
d. silk

A

a. Collagen

72
Q

Which has a high content of proline?
a. collagen
b. keratin
c. myoglobin
d. silk

A

a. collagen

73
Q

Bone tendon contains which of the following:
a. collagen
b. keratin
c. myoglobin
d. silk

A

a. Collagen

74
Q

British sailors were given lime juice in the age of sail to prevent which disease?

A

Scurvy

75
Q

Which region of the diffraction pattern gives the highest resolution in crystallography?
a. 1
b. 2
c. 3
d. 4

A

1 (outermost region)

76
Q

Which is NOT an advantage of crystallography?

a. can obtain the structure of large macromolecules and complexes
b. can get the position of AA sidechains
c. Determined structure is dynamic
d. can get to 4.5 angstroms resolution

A

c. Determined structure is dynamic

77
Q

Which protein denaturing method associates with nonpolar amino acids blocking water interactions?
a. heat
b. detergents
c. pH
d. Chaotropes

A

b. Detergents

78
Q

Which method can solve the phase problem of crystallography?
a. Isomorphous replacement
b. Direct methods
c. Molecular replacement
d. all of the above

A

d. all of the above

79
Q

There is an estimate of about how many different folding motifs for proteins:
a. 50
b. 100
c. 500
d. 1000

A

1000

80
Q

Which amino acid is the most hydrophobic?
a. Asp
b. Gly
c. His
d. Val

A

d. Val

Val, she’s scared of water

81
Q

The GroESL (chaperonin) system uses how many ATP when refolding a protein?
a. 2
b. 10
c. 14
d. 28

A

14

82
Q

Which of the following is true regarding SDS-PAGE gels?
a. the proteins that run on the gel have a negative charge
b. the proteins are separated according to molecular weight
c. the proteins run on the gel are in their native conformation
d. two of the above (a and b)

A

d. two of the above (a and b)

83
Q

What is required for hydroxyproline formation?
a. Thiamin
b. Cobalamin
c. Ascorbic Acid
d. Nicotinic Acid

A

c. Ascorbic Acid

84
Q

What is true of peptide bonds?
a. most assume a cis conformation
b. they have ~60% double bond character
c. they are planar
d. none of the above

A

They are planar

85
Q

Which amino acid has the highest propensity for a helical conformation?
a. P
b. G
c. C
d. A

A

P(Proline)

86
Q

Which amino acid has the highest propensity for beta sheet conformation?
a. E
b. V
c. P
d. S

A

E (Glutamate)

87
Q

What advantage(s) does NMR provide over X-ray crystallography in characterizing protein structure?
a. NMR can be used for proteins that don’t crystallize
b. NMR can be used for proteins over 200 kDa
c. Both A and B
d. None of the above

A

a. NMR can be used for proteins that don’t crystallize

88
Q

Which is composed of mostly beta sheets?
a. Collagen
b. Keratin
c. Myoglobin
d. Silk

A

d. Silk

think how strong silk is and structure of beta sheets

89
Q

Ni2+ columns bonds to poly histidine residue tags placed onto a protein for purification, what kind of purification is this considered?
a. Affinity purification
b. Ion exchange
c. Phase separation
d. size exclusion

A

a. Affinity purification

90
Q

You have a protein with a pI of 9. You are running at pH of 7.2. Which would be the best type of resin should you use to purify it?
a. anion exchange resin
b. cation exchange resin
c. Ni2+ resin
d. size exclusion resin

A

b. Cation Exchange Resin

91
Q

Which amino acid would Trypsin cleave at:
a. Arg
b. Leu
c. Met
d. Phe

A

Arg

92
Q

Which protein denaturing method solubilizes hydrophobic region of proteins?
a. heat
b. detergents
c. pH
d. chaotropes

A

Chaotropes

93
Q

Given the following chart and an amino acid sequence of RCIVWRMQTY, what is the most likely secondary structure to form?

A

Alpha helix

94
Q

Which amino acid is least likely to be found on the exterior of the protein?
a. Ser
b. Lys
c. Met
d. Asn

A

Met

95
Q

What do vertical grey lines denote about the amino acid position? The amino acid position may be important:
a. enzymatic
b. structurally
c. for binding small molecules
d. all of the above

A

d. all of the above

96
Q

Which filament protein has crosslinked Lys?
a. collagen
b. keratin
c. silk
d. none of the above

A

Collagen

97
Q

Which protein is unable to expand due to its structure?
a. collagen
b. keratin
c. silk
d. none of the above

A

Silk

98
Q

Which protein forms bone?
a. collagen
b. keratin
c. silk
d. none of the above

A

Collagen

99
Q

Which is a drawback of crystallography?
a. You need to find crystallization conditions
b. The structure is static
c. You have to determine the phase of the crystal
d. All of the above

A

d. All of the above

100
Q

What is an advantage compared to x-ray crystallography?
a. able to easily determine structure of 20kDa proteins
b. Able to determine the structure of membrane proteins
c. Able to get resolutions at 1.5 angstroms
d. able to get dynamic structures

A

Able to determine the structure of membrane proteins

101
Q

An advantage of NMR is:
a. large proteins structure can be determined
b. the structure is dynamic
c. all side chains are well defined
d. proteins must be labeled

A

b. The structure is dynamic

102
Q

Which is a beta hairpin turn?
a. A
b. B
c. C
d. Not shown

A

B (figure 6.8b)
consists of antiparallel strands connected by relatively tight reverse turns

103
Q

About how many folds do half the proteins fit into?
A. 30
B. 100
C. 300
D. 1000

A

30

104
Q

A protein’s structure is determined by its:
a. bound molecules
b. enzymatic activity
c. primary structure
d. secondary structure

A

c. Primary structure

105
Q

The GroESL protein folding system takes about how much energy (kJ/mol) to refold a protein?
a. 21
b. 42
c. 210
d. 420

A

d. 420

106
Q

Which disease is caused by misfolded proteins?
a. Osteogenesis imperfecta
b. Prions
c. Scurvy
d. Sickle Cell Anemia

A

b. Prions

107
Q

In what order would Arg, Asp, Cys, and Ser be eluted from a diethylaminoethyl column at pH 8.5?

A

ASCA
Arg, Ser, Cys, Asp

108
Q

Protein Y has an absorptivity of 0.5 mL-mg-1-cm at 280 nm. What is the absorbance at 280 nm of a 2mg-mL-1 solution of protein Y?

A

1

(0.5 mL)(2 mg-mL)

109
Q

Protein Y has an absorptivity of 0.06 mL-mg-1-cm-1 at 280 nm. What is the absorbance at 280 nm of a 4.0 mg mL-1 solution?

A

0.24

(0.06 mL)(4.0 mg-mL)

BCHS (7 decks)

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