This Study Resource Was: Chapter 3 Exploring Proteins and Proteomes

Chapter 3 Exploring Proteins and Proteomes
Multiple-Choice Questions
1) The ratio of enzyme activity relative to total protein is called _____.
A) inherent activity
B) specific activity
C) explicit activity
D) exclusive activity
E) purified activity
Answer: B
Section: 3.1
m
er as
2) Which of the following is often the first step in protein purification from a homogenate?
co
eH w
A) ion exchange chromatography
B) gel-filtration chromatography
o.
C) HPLC
D) centrifugation rs e
ou urc
E) gel electrophoresis
Answer: D
o
Section: 3.1
aC s
vi y re
3) Which type of protein purification relies on the attraction of the protein for a particular
chemical group?
A) affinity chromatography
ed d
B) gel-filtration chromatography
ar stu
C) HPLC
D) gel electrophoresis
E) isoelectric focusing
is
Answer: A
Th
Section: 3.1
4) _____ can be added prior to gel electrophoresis to fully denature proteins.

sh
A) Coomassie blue
B) polyacrylamide
C) SDS
D) -mercaptoethanol
E) All of the answers are correct.
This study source was downloaded by 100000830124955 from CourseHero.com on 11-22-2021 12:22:48 GMT -06:00
https://www.coursehero.com/file/19573839/berg-8e-testbank-chapter031/
Chapter 3 Exploring Proteins and Proteomes 2
Answer: D
Section: 3.1
5) The unit for sedimentation coefficients is the _____.
A) Newton
B) radian
C) g
D) Svedberg
E) None of the answers is correct.
Answer: D
Section: 3.1
6) What technique would be used to separate proteins with different sedimentation
m
er as
coefficients?
co
eH w
A) MALDI-TOF mass spectrometry
B) zonal centrifugation
o.
C) HPLC
D) rs e
gel-filtration chromatography
ou urc
Answer: B
o
Section: 3.1
aC s
vi y re
7) Which of the following are used to sequence entire proteins?
A) affinity peptides
B) circular peptides
ed d
C) overlap peptides
ar stu
D) labeled peptides
E) synthetic peptides
is
Answer: C
Section: 3.3
Th
8) _____ is the term to describe an original amino acid sequence for an uncleaved protein.
A) Apoprotein
sh
B) Holoprotein
C) Nascent
D) Protomer
E) None of the answers is correct.
Answer: C
Section: 3.3
9) What technique can be used to determine the mass of a protein without knowing the
identity of the molecule?
A) affinity chromatography
B) ion exchange chromatography
C) polyacrylamide gel electrophoresis
D) MALDI-TOF mass spectrometry
E) western blot
Answer: D
Section: 3.3
10) Another name for an antigenic determinant is _____.
m
er as
A) epitope
co
eH w
B) epimer
C) epinephrine
o.
D) epidemic
E) rs e
None of the answers is correct.
ou urc
Answer: A
Section: 3.2
o
aC s
vi y re
Fill-in-the-Blank Questions
11) Proteins can be separated from small molecules and ions through a semipermeable membrane
ed d
by __________________.
ar stu
Ans: dialysis Section: 3.1
12) Molecular exclusion or gel-filtration chromatography separates molecules on the basis of

__________________.
is
Ans: size Section: 3.1

Th
13) Dithiothreitol or β mercaptoethanol are commonly used to reduce _______________ bonds.

Ans: disulfide Section: 3.1
sh
14) In the Edman procedure for peptide sequence, phenyl isothiocyanate is used to selectively
remove the __________________ residue as a PTH-derivative.
Ans: N-terminal Section: 3.3
15) Long proteins are often treated with the enzyme ______________, which cleaves the protein
into smaller, easily analyzed peptides.
Ans: trypsin OR chymotrypsin OR thrombin Section: 3.3
16) Mass spectrometric techniques are critical in _________________research, which explores the
proteins present in a cell, because it is possible to analyze constituents of large macromolecular
assemblies.
Ans: proteomics Section: 3.3
17) The advantage to ______________________protein synthesis is that the desired product is

bound to beads and excess reagents can be easily removed at each step.
Ans: solid-phase Section: 3.4
18) Polypeptides can be fragmented into smaller peptides by cleavage with trypsin, which
hydrolyzes the peptide bond at the C-terminal side of __________________ residues.
Ans: lysine and arginine OR Lys and Arg OR K and R Section: 3.3
19) __________________ gels are often used as the media for electrophoretic techniques such as
SDS-PAGE and isoelectric focusing.
Ans: Polyacrylamide Section: 3.1
m
er as
20) The mobility of proteins in SDS-PAGE is inversely proportional to the _____________.
co
Ans: logarithm of their mass OR log of their molecular weight Section: 3.1
eH w
o.
Multiple-Choice Questions
rs e
ou urc
21) When enzymes are purified, the assay is often based on
A) light absorbance. D) temperature changes.
B) catalytic activity. E) mRNA levels.
o
C) pH.
aC s
Ans: B Section: 3.1

vi y re
22) Proteins that are not catalysts are often probed or assayed using
A) antibody binding assays. D) None of the answers is correct.
B) catalytic activity. E) All of the answers are correct.
ed d
C) genomic analysis.
ar stu
Ans: A Section: 3.2
23) What is the advantage of adding SDS to gel electrophoresis?

A) SDS colors the proteins for visualization.
is
B) SDS reduces disulfide bonds.

Th
C) SDS allows proteins to be separated on the basis of approximate mass.

D) None of the answers is correct.
Ans: C Section: 3.1
sh
24) Two-dimensional electrophoresis is a combination of what two techniques?

A) ion-exchange chromatography and affinity chromatography
B) ion-exchange chromatography and SDS-PAGE
C) SDS-PAGE and affinity chromatography
D) isoelectric focusing and SDS-PAGE
E) isoelectric focusing and ion-exchange chromatography
Ans: D Section: 3.1
25) Which of the following affect the sedimentation rate of a particle?

A) mass D) All of the answers are correct.
B) shape E) mass and shape
C) the density of the solution
Ans: D Section: 3.1
26) Cyanogen bromide cleaves the peptide bond at

A) the carboxyl side of Arg and Lys residues.
B) the carboxyl side of Met residues.
C) the amino terminus.
Ans: B Section: 3.3
m
27) Protein databases
er as
A) can identify proteins from small stretches of amino acid sequences.
co
B) are not useful in proteomics studies due to the complexities of the proteome.
eH w
C) are determined from sequence data only, never deduced from genomic data.
o.
E)
rs e
All of the answers are correct.
Ans: A Section: 3.3
ou urc
28) Which of the following techniques can be used to determine mass to charge ratio of a molecule?
A) Edman degradation D) MALDI-TOF
o
B) affinity chromatography E) SDS-PAGE

aC s
C) diagonal electrophoresis
vi y re
Ans: D Section: 3.3
29) What types of molecules can serve as antigens?

A) proteins D) All of the answers are correct.
ed d
B) polysaccharides E) proteins and polysaccharides

ar stu
C) metal ions
Ans: E Section: 3.2
30) An ELISA can be used for

is
A) quantitative analysis. D) All of the answers are correct.

B) size analysis. E) None of the answers is correct.
Th
C) protein sequencing
Ans: A Section: 3.2
31) A technique used to identify proteins after gel electrophoresis, which employs antibodies in the
sh
detection process, is known as

A) northern blot D) Southern blot
B) southwestern blot E) None of the answers is correct.
C) western blot
Ans: C Section: 3.2
32) A technique that can be used to study three-dimensional protein structure is

A) one-dimensional NMR spectroscopy D) Western blotting
B) fluorescent microscopy E) ion-exchange chromatography
C) x-ray crystallography
Ans: C Section: 3.5
33) The use of synthetic peptides includes

A) use as antigens for making antibodies.
B) drugs.
C) “hooks” for use in affinity purification.
D) All of the answers are correct.
E) use as antigens for making antibodies and “hooks” for use in affinity purification.
Ans: D Section: 3.4
34) Which technique cannot be used for quantitative analysis?

A) x-ray crystallography D) All of the answers are correct.
B) ELISA E) None of the answers is correct.
m
C) absorbance spectroscopy
er as
Ans: A Section: Entire Chapter
co
eH w
35) Techniques that can be used to obtain information about protein shape are
o.
A) x-ray crystallography. D) x-ray crystallography and NOESY NMR
B) rs e
NOESY NMR spectroscopy. E)
spectroscopy.
All the answers are correct.
ou urc
C) SDS-PAGE.
Ans: D Section: 3.5
o
aC s
Short-Answer Questions
vi y re
36) Why is an assay necessary for protein purification studies?

Ans: An assay allows researchers to accurately measure the amount of the desired protein
which allows the researcher to track the protein during the purification process. This is
ed d
important in determining if particular purification steps are effective in isolating the

ar stu
protein from the other cellular material.

Section: 3.1
37) How is lactate dehydrogenase assayed?

is
Ans: It is assayed by the increase in NADH present. NADH has a unique absorbance at 340
nm, and the reaction can be monitored by the increase in absorbance at this wavelength.
Th
Section: 3.1
38) How do gel-filtration and ion-exchange chromatography differ?

Ans: Although both are used in purification, the properties of the column material determine
sh
how the separation is accomplished. Gel filtration is based on porous beads, and
molecules are separated by size, largest molecules eluting first. In ion-exchange
chromatography, the column material is charged with either positively or negatively
charged molecules. Separation is based on the protein’s charge which dictates its affinity
for the column media. Protein affinity to ion-exchange column material can be
manipulated by altering the pH.
Section: 3.1
39) How can a protein’s isoelectric point be used in protein purification (i.e., isoelectric focusing)?
Ans: Isoelectric focusing is an electrophoretic technique in which a gradient charge is applied.
Proteins migrate through the gradient field until they reach a point at which the pH is the
same as the protein’s pI.
Section: 3.1
40) What is the purpose of determining the specific activity, yield, and purification level of a protein
purification protocol?
Ans: The measurements allow one to determine if the individual steps were effective at
selectively isolating the protein while maintaining its presence and activity. In order to
successfully purify protein, both the yield and purification level must remain high.
Section: 3.1
41) What type of information can be obtained from ultracentrifugation?

Ans: This technique can be used to determine mass and density and to investigate molecular
m
shape and molecular interactions.
er as
Section: 3.1
co
eH w
42) How can recombinant DNA technology aid in protein purification?
o.
Large quantities of proteins can be expressed, allowing for extensive characterization of
rs e
Ans: the protein. Affinity tags can be fused to the protein to aid in solid phase studies. Mature
ou urc
proteins that have already been modified can be generated.
Section: 3.1
43) Describe the Edman degradation method for protein-sequence analysis.

o
Ans: A pure protein is reacted with phenyl isothiocyanate (PITC), which binds to the free
aC s
amino terminus. Under mildly acidic conditions, the derivatized amino acid is liberated,
vi y re
and can be identified by chromatography. The steps are repeated to identify the next
amino acid exposed at the amino terminus. The process is only reliable for <50 amino
acids.
Section: 3.3
ed d
ar stu
44) How can the amino acid sequences be used to design a DNA probe?
Ans: Using the amino acid sequence and the genetic code, a DNA sequence can be designed.
(Codon degeneracy, i.e., multiple codons encoding the same amino acid, must be
considered in the design.)
is
Section: 3.3
Th
45) What is one advantage of using the recombinant DNA methods to determine protein sequences?
Ans: Large proteins can be difficult to sequence by traditional methods because only short
peptides can be sequenced. Long sections of DNA can be cloned and sequenced, with the
genetic code used to determine the amino acid sequence.
sh
Section: 3.3
46) After a protein is purified, what is the next step in determining the structure of a protein by x-ray
crystallography?
Ans: The next step is to prepare a protein in a crystal form, in which all protein molecules are
oriented in a fixed, repeated arrangement.
Section: 3.5
47) Why are monoclonal antibodies more useful than polyclonal antibodies?
Ans: Monoclonal antibodies are more specific, consisting of one type of antibody with a
specific binding site and affinity. Polyclonal antibodies contain several different
antibodies with slightly different binding affinities and specificities. Monoclonal
antibodies are more suitable for examining protein structure and studying mechanisms.
Section: 3.2
48) How are monoclonal antibodies made?

Ans: They are made by fusion of an immortal myeloma cell line with a short-lived, antibody-
producing cell.
Section: 3.2
49) Briefly describe how an ELISA works.

Ans: In ELISA, the antigen of interest is complexed with a specific antibody under appropriate
assay conditions, and excess antibody is removed. The antibody is complexed to an
m
enzyme, which can be measured quantitatively using an appropriate substrate and assay
er as
tool, often by a colorimetric product formation.
co
Section: 3.2
eH w
o.
50) What are some of the advantages and drawbacks of NMR spectroscopy compared to x-ray
crystallography?
rs e
ou urc
Ans: While both are expensive and time-consuming techniques, NMR allows the native
structure of the protein in solution to be determined. Not all proteins readily form crystals
so NMR can be used to study the structure of these proteins. Currently, one major
drawback is that NMR can only be used to study small proteins with low molecular
o
weights (<40kDa).
aC s
Section: 3.5
vi y re
ed d
ar stu
is
Th
sh
Powered by TCPDF (www.tcpdf.org)

This Study Resource Was: Chapter 3 Exploring Proteins and Proteomes

Uploaded by

Document Information

Original Title

Copyright

Available Formats

Share this document

Share or Embed Document

Sharing Options

Did you find this document useful?

Is this content inappropriate?

Copyright:

Available Formats

This Study Resource Was: Chapter 3 Exploring Proteins and Proteomes

Uploaded by

Copyright:

Available Formats

Chapter 3 Exploring Proteins and Proteomes

1) The ratio of enzyme activity relative to total protein is called _____.

4) _____ can be added prior to gel electrophoresis to fully denature proteins.

5) The unit for sedimentation coefficients is the _____.

6) What technique would be used to separate proteins with different sedimentation

7) Which of the following are used to sequence entire proteins?

10) Another name for an antigenic determinant is _____.

Ans: dialysis Section: 3.1

12) Molecular exclusion or gel-filtration chromatography separates molecules on the basis of

Ans: size Section: 3.1

13) Dithiothreitol or β mercaptoethanol are commonly used to reduce _______________ bonds.

17) The advantage to ______________________protein synthesis is that the desired product is

Ans: B Section: 3.1

Ans: A Section: 3.2

23) What is the advantage of adding SDS to gel electrophoresis?

B) SDS reduces disulfide bonds.

C) SDS allows proteins to be separated on the basis of approximate mass.

24) Two-dimensional electrophoresis is a combination of what two techniques?

Ans: D Section: 3.1

25) Which of the following affect the sedimentation rate of a particle?

26) Cyanogen bromide cleaves the peptide bond at

B) affinity chromatography E) SDS-PAGE

Ans: D Section: 3.3

29) What types of molecules can serve as antigens?

B) polysaccharides E) proteins and polysaccharides

30) An ELISA can be used for

A) quantitative analysis. D) All of the answers are correct.

detection process, is known as

32) A technique that can be used to study three-dimensional protein structure is

33) The use of synthetic peptides includes

34) Which technique cannot be used for quantitative analysis?

36) Why is an assay necessary for protein purification studies?

important in determining if particular purification steps are effective in isolating the

protein from the other cellular material.

37) How is lactate dehydrogenase assayed?

38) How do gel-filtration and ion-exchange chromatography differ?

41) What type of information can be obtained from ultracentrifugation?

43) Describe the Edman degradation method for protein-sequence analysis.

48) How are monoclonal antibodies made?

49) Briefly describe how an ELISA works.

You might also like