Question 1

The advantage of using an SDS-PAGE gel compared with a native PAGE gel is that the SDS-PAGE gel

Accepted Answer

A)  separates proteins only based on molar mass. 
B)  gives information about the charge or conformation of the protein. 
C)  results in a better separation of small proteins. 
D)  increases the resolution of large and small proteins. 
A)  separates proteins only based on molar mass. 
B)  gives information about the charge or conformation of the protein. 
C)  results in a better separation of small proteins. 
D)  increases the resolution of large and small proteins.

Question 2

What are the advantages of using a monoclonal antibody compared with a polyclonal antibody?

Accepted Answer

Monoclonal antibodies are generated from

Question 3

Biochemical assays are important in the process of isolating proteins because they

Accepted Answer

A)  uniquely identify one protein. 
B)  separate proteins based on polarity. 
C)  isolate proteins based on size. 
D)  determine the molecular weight of proteins. 
A)  uniquely identify one protein. 
B)  separate proteins based on polarity. 
C)  isolate proteins based on size. 
D)  determine the molecular weight of proteins.

Question 4

Why is it more advantageous to use Edman degradation instead of Sanger's sequencing method?

Accepted Answer

Sanger's method requires adding fresh pr

Question 5

The size of proteins studied by NMR is limited because

Accepted Answer

A)  a small sample size is needed. 
B)  it is hard to determine the phases of diffracted X-rays. 
C)  the measurements of the distances between atoms are only approximate. 
D)  large molecules reorient slowly in solution. 
A)  a small sample size is needed. 
B)  it is hard to determine the phases of diffracted X-rays. 
C)  the measurements of the distances between atoms are only approximate. 
D)  large molecules reorient slowly in solution.

Question 6

Which technique ionizes polypeptides by releasing them from a small metallic capillary at high voltage?

Accepted Answer

A)  ESI 
B)  MALDI 
C)  NMR 
D)  X-ray crystallography 
A)  ESI 
B)  MALDI 
C)  NMR 
D)  X-ray crystallography

Question 7

Theoretically, an individual B cell could express any combination of light chain and heavy chain polypeptides to produce one of 10 antibody complexes. How does this seemingly limited production of antibodies protect us from the tens of millions of foreign antigens we encounter through our lives?

Accepted Answer

DNA recombination is the reason that we

Question 8

During the production of polyclonal antibodies, how are the antigen-specific antibodies purified?

Accepted Answer

A)  dialysis 
B)  gel electrophoresis 
C)  size exclusion chromatography 
D)  affinity chromatography 
A)  dialysis 
B)  gel electrophoresis 
C)  size exclusion chromatography 
D)  affinity chromatography

Question 9

Which peptide would migrate the fastest in a SDS-PAGE gel?

Accepted Answer

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

Question 10

In an ELISA, the detection antibody is a antibody.

Accepted Answer

A)  monoclonal primary 
B)  polyclonal tertiary 
C)  monoclonal secondary 
D)  polyclonal secondary 
A)  monoclonal primary 
B)  polyclonal tertiary 
C)  monoclonal secondary 
D)  polyclonal secondary

Question 11

The figure below shows how differential centrifugation can be used to isolate four subcellular fractions. Which fraction corresponds to the mitochondrial fraction?

Accepted Answer

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

Question 12

Immunoprecipitation uses an antibody-bead combination to

Accepted Answer

A)  detect the antigen. 
B)  enrich the protein solution. 
C)  digest the proteins for use in mass spectrometry. 
D)  separate the proteins using centrifugation. 
A)  detect the antigen. 
B)  enrich the protein solution. 
C)  digest the proteins for use in mass spectrometry. 
D)  separate the proteins using centrifugation.

Question 13

The following peptides are separated using an anion exchange resin in ion-exchange chromatography. Which peptide is eluted first?

Accepted Answer

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

Question 14

Explain the difference between polyclonal and monoclonal antibodies.

Accepted Answer

A polyclonal antibody is a heterogeneous

Question 15

Which separation technique exploits the solubility differences of proteins?

Accepted Answer

A)  centrifugation 
B)  salting out 
C)  dialysis 
D)  ion-exchange chromatography 
A)  centrifugation 
B)  salting out 
C)  dialysis 
D)  ion-exchange chromatography

Question 16

Below are the steps of a Western blot. What is the correct order? 1. The membrane is incubated with the secondary antibody.
2) The membrane is incubated with the primary antibody.
3) The membrane is washed with a blocking solution.
4) Proteins are transferred to a nitrocellulose membrane.
5) Protein extracts are separated by gel electrophoresis.

Accepted Answer

A)  5, 4, 3, 2, 1 
B)  4, 5, 2, 3, 1 
C)  3, 4, 5, 1, 2 
D)  2, 5, 4, 3, 1 
A)  5, 4, 3, 2, 1 
B)  4, 5, 2, 3, 1 
C)  3, 4, 5, 1, 2 
D)  2, 5, 4, 3, 1

Question 17

Explain how to separate the following proteins using two different types of chromatography.

Accepted Answer

Use size exclusion chromatography to sep

Question 18

The figure below shows how differential centrifugation can be used to isolate four subcellular fractions. Which fraction corresponds to the membrane fraction?

Accepted Answer

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

Question 19

Explain the difference between the primary and secondary antibody using a Western blot.

Accepted Answer

The primary antibody facilitates the ant

Question 20

Polyclonal antibodies are

Accepted Answer

A)  derived from B cells isolated from the spleen. 
B)  isolated from hybridoma cells. 
C)  a heterogeneous mixture. 
D)  a homogenous mixture. 
A)  derived from B cells isolated from the spleen. 
B)  isolated from hybridoma cells. 
C)  a heterogeneous mixture. 
D)  a homogenous mixture.

The advantage of using an SDS-PAGE gel compared with a native PAGE gel is that the SDS-PAGE gel

What are the advantages of using a monoclonal antibody compared with a polyclonal antibody?

Biochemical assays are important in the process of isolating proteins because they

Why is it more advantageous to use Edman degradation instead of Sanger's sequencing method?

The size of proteins studied by NMR is limited because

Which technique ionizes polypeptides by releasing them from a small metallic capillary at high voltage?

Theoretically, an individual B cell could express any combination of light chain and heavy chain polypeptides to produce one of 10 antibody complexes. How does this seemingly limited production of antibodies protect us from the tens of millions of foreign antigens we encounter through our lives?

During the production of polyclonal antibodies, how are the antigen-specific antibodies purified?

Which peptide would migrate the fastest in a SDS-PAGE gel?

In an ELISA, the detection antibody is a antibody.

Immunoprecipitation uses an antibody-bead combination to

The following peptides are separated using an anion exchange resin in ion-exchange chromatography. Which peptide is eluted first?

Explain the difference between polyclonal and monoclonal antibodies.

Which separation technique exploits the solubility differences of proteins?

Explain how to separate the following proteins using two different types of chromatography.

Explain the difference between the primary and secondary antibody using a Western blot.

Polyclonal antibodies are

Principles of Biochemistry

Physical Biochemistry: Energy Conversion, Water, and Membranes

Nucleic Acid Structure and Function

Protein Structure

Protein Function

Enzyme Mechanisms

Cell Signaling Systems

Glycolysis: a Paradigm of Metabolic Regulation

The Citrate Cycle

Oxidative Phosphorylation

Photosynthesis

Carbohydrate Structure and Function

Carbohydrate Metabolism

Lipid Structure and Function

Lipid Metabolism

Amino Acid Metabolism

Nucleotide Metabolism

Metabolic Integration

DNA Replication, Repair, and Recombination

RNA Synthesis, Processing, and Gene Silencing

Protein Synthesis, Posttranslational Modification, and Transport

Gene Regulation

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Exam 5: Methods in Protein Biochemistry

The advantage of using an SDS-PAGE gel compared with a native PAGE gel is that the SDS-PAGE gel

What are the advantages of using a monoclonal antibody compared with a polyclonal antibody?

Biochemical assays are important in the process of isolating proteins because they

Why is it more advantageous to use Edman degradation instead of Sanger's sequencing method?

The size of proteins studied by NMR is limited because

Which technique ionizes polypeptides by releasing them from a small metallic capillary at high voltage?

Theoretically, an individual B cell could express any combination of light chain and heavy chain polypeptides to produce one of 10 antibody complexes. How does this seemingly limited production of antibodies protect us from the tens of millions of foreign antigens we encounter through our lives?

During the production of polyclonal antibodies, how are the antigen-specific antibodies purified?

Which peptide would migrate the fastest in a SDS-PAGE gel?

In an ELISA, the detection antibody is a antibody.

The figure below shows how differential centrifugation can be used to isolate four subcellular fractions. Which fraction corresponds to the mitochondrial fraction?

Immunoprecipitation uses an antibody-bead combination to

The following peptides are separated using an anion exchange resin in ion-exchange chromatography. Which peptide is eluted first?

Explain the difference between polyclonal and monoclonal antibodies.

Which separation technique exploits the solubility differences of proteins?

Explain how to separate the following proteins using two different types of chromatography.

The figure below shows how differential centrifugation can be used to isolate four subcellular fractions. Which fraction corresponds to the membrane fraction?

Explain the difference between the primary and secondary antibody using a Western blot.

Polyclonal antibodies are

Principles of Biochemistry

Physical Biochemistry: Energy Conversion, Water, and Membranes

Nucleic Acid Structure and Function

Protein Structure

Protein Function

Enzyme Mechanisms

Cell Signaling Systems

Glycolysis: a Paradigm of Metabolic Regulation

The Citrate Cycle

Oxidative Phosphorylation

Photosynthesis

Carbohydrate Structure and Function

Carbohydrate Metabolism

Lipid Structure and Function

Lipid Metabolism

Amino Acid Metabolism

Nucleotide Metabolism

Metabolic Integration

DNA Replication, Repair, and Recombination

RNA Synthesis, Processing, and Gene Silencing

Protein Synthesis, Posttranslational Modification, and Transport

Gene Regulation

Filters