Question 1

Proteins that are not catalysts are often probed or assayed using

Accepted Answer

A)  antibody binding assays. 
B)  catalytic activity. 
C)  genomic analysis. 
D)  None of the answers is correct. 
E)  All of the answers are correct. 
A)  antibody binding assays. 
B)  catalytic activity. 
C)  genomic analysis. 
D)  None of the answers is correct. 
E)  All of the answers are correct.

Question 2

The advantage to ______________________protein synthesis is that the desired product is bound to beads and excess reagents can be easily removed at each step.

Accepted Answer

The answer of The advantage to ______________________protein synthesis is that...

Question 3

_____ is the term to describe an original amino acid sequence for an uncleaved protein.

Accepted Answer

A)  Apoprotein 
B)  Holoprotein 
C)  Nascent 
D)  Protomer 
E)  None of the answers is correct. 
A)  Apoprotein 
B)  Holoprotein 
C)  Nascent 
D)  Protomer 
E)  None of the answers is correct.

Question 4

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.

Accepted Answer

The answer of Mass spectrometric techniques are critical in _________________research,...

Question 5

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

Accepted Answer

A)  inherent activity 
B)  specific activity 
C)  explicit activity 
D)  exclusive activity 
E)  purified activity 
A)  inherent activity 
B)  specific activity 
C)  explicit activity 
D)  exclusive activity 
E)  purified activity

Question 6

How can the amino acid sequences be used to design a DNA probe?

Accepted Answer

Using the amino acid sequence

Question 7

Techniques that can be used to obtain information about protein shape are

Accepted Answer

A)  x-ray crystallography. 
B)  NOESY NMR spectroscopy. 
C)  SDS-PAGE. 
D)  x-ray crystallography and NOESY NMR spectroscopy. 
E)  All the answers are correct. 
A)  x-ray crystallography. 
B)  NOESY NMR spectroscopy. 
C)  SDS-PAGE. 
D)  x-ray crystallography and NOESY NMR spectroscopy. 
E)  All the answers are correct.

Question 8

What is the purpose of determining the specific activity, yield, and purification level of a protein purification protocol?

Accepted Answer

The measurements allow one to determine

Question 9

Protein databases

Accepted Answer

A)  can identify proteins from small stretches of amino acid sequences. 
B)  are not useful in proteomics studies due to the complexities of the proteome. 
C)  are determined from sequence data only, never deduced from genomic data. 
D)  None of the answers is correct. 
E)  All of the answers are correct. 
A)  can identify proteins from small stretches of amino acid sequences. 
B)  are not useful in proteomics studies due to the complexities of the proteome. 
C)  are determined from sequence data only, never deduced from genomic data. 
D)  None of the answers is correct. 
E)  All of the answers are correct.

Question 10

The unit for sedimentation coefficients is the _____.

Accepted Answer

A)  Newton 
B)  radian 
C)  g 
D)  Svedberg 
E)  None of the answers is correct. 
A)  Newton 
B)  radian 
C)  g 
D)  Svedberg 
E)  None of the answers is correct.

Question 11

What technique can be used to determine the mass of a protein without knowing the identity of the molecule?

Accepted Answer

A)  affinity chromatography 
B)  ion exchange chromatography 
C)  polyacrylamide gel electrophoresis 
D)  MALDI-TOF mass spectrometry 
E)  western blot 
A)  affinity chromatography 
B)  ion exchange chromatography 
C)  polyacrylamide gel electrophoresis 
D)  MALDI-TOF mass spectrometry 
E)  western blot

Question 12

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

Accepted Answer

The answer of Dithiothreitol or β mercaptoethanol are commonly used...

Question 13

Why are monoclonal antibodies more useful than polyclonal antibodies?

Accepted Answer

Monoclonal antibodies are more specific,

Question 14

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

Accepted Answer

Although both are used in purification,

Question 15

Which of the following are used to sequence entire proteins?

Accepted Answer

A)  affinity peptides 
B)  circular peptides 
C)  overlap peptides 
D)  labeled peptides 
E)  synthetic peptides 
A)  affinity peptides 
B)  circular peptides 
C)  overlap peptides 
D)  labeled peptides 
E)  synthetic peptides

Question 16

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

Accepted Answer

A)  Coomassie blue 
B)  polyacrylamide 
C)  SDS 
D)  $\beta$-mercaptoethanol 
E)  All of the answers are correct. 
A)  Coomassie blue 
B)  polyacrylamide 
C)  SDS 
D)  $\beta$-mercaptoethanol 
E)  All of the answers are correct.

Question 17

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

Accepted Answer

A)  one-dimensional NMR spectroscopy 
B)  fluorescent microscopy 
C)  x-ray crystallography 
D)  Western blotting 
E)  ion-exchange chromatography 
A)  one-dimensional NMR spectroscopy 
B)  fluorescent microscopy 
C)  x-ray crystallography 
D)  Western blotting 
E)  ion-exchange chromatography

Question 18

A technique used to identify proteins after gel electrophoresis, which employs antibodies in the detection process, is known as

Accepted Answer

A)  northern blot 
B)  southwestern blot 
C)  western blot 
D)  Southern blot 
E)  None of the answers is correct. 
A)  northern blot 
B)  southwestern blot 
C)  western blot 
D)  Southern blot 
E)  None of the answers is correct.

Question 19

What types of molecules can serve as antigens?

Accepted Answer

A)  proteins 
B)  polysaccharides 
C)  metal ions 
D)  All of the answers are correct. 
E)  proteins and polysaccharides 
A)  proteins 
B)  polysaccharides 
C)  metal ions 
D)  All of the answers are correct. 
E)  proteins and polysaccharides

Question 20

Which of the following techniques can be used to determine mass to charge ratio of a molecule?

Accepted Answer

A)  Edman degradation 
B)  affinity chromatography 
C)  diagonal electrophoresis 
D)  MALDI-TOF 
E)  SDS-PAGE 
A)  Edman degradation 
B)  affinity chromatography 
C)  diagonal electrophoresis 
D)  MALDI-TOF 
E)  SDS-PAGE

Exam 3: Exploring Proteins and Proteomes

Proteins that are not catalysts are often probed or assayed using

The advantage to ______________________protein synthesis is that the desired product is bound to beads and excess reagents can be easily removed at each step.

_____ is the term to describe an original amino acid sequence for an uncleaved protein.

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.

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

How can the amino acid sequences be used to design a DNA probe?

Techniques that can be used to obtain information about protein shape are

What is the purpose of determining the specific activity, yield, and purification level of a protein purification protocol?

Protein databases

The unit for sedimentation coefficients is the _____.

What technique can be used to determine the mass of a protein without knowing the identity of the molecule?

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

Why are monoclonal antibodies more useful than polyclonal antibodies?

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

Which of the following are used to sequence entire proteins?

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

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

A technique used to identify proteins after gel electrophoresis, which employs antibodies in the detection process, is known as

What types of molecules can serve as antigens?

Which of the following techniques can be used to determine mass to charge ratio of a molecule?

Biochemistry: an Evolving Science

Protein Composition and Structure

DNA, RNA, and the Flow of Genetic Information

Exploring Genes and Genomes

Exploring Evolution and Bioinformatics

Hemoglobin: a Portrait of a Protein in Action

Enzymes: Basic Concepts and Kinetics

Oxidative Phosphorylation

Catalytic Strategies

Regulatory Strategies

Carbohydrates

Lipids and Cell Membranes

Membrane Channels and Pumps

Signal-Transduction Pathways

Metabolism: Basic Concepts and Design

Glycolysis and Gluconeogenesis

The Citric Acid Cycle

The Light Reactions of Photosynthesis

The Calvin Cycle and the Pentose Phosphate Pathway

Glycogen Metabolism

Fatty Acid Metabolism

Protein Turnover and Amino Acid Catabolism

The Biosynthesis of Amino Acids

Nucleotide Biosynthesis

Biosynthesis of Membrane Lipids and Steroids

The Integration of Metabolism

DNA Replication, Repair, and Recombination

Rna Synthesis and Processing

Protein Synthesis

The Control of Gene Expression in Prokaryotes

The Control of Gene Expression in Eukaryotes

Sensory Systems

The Immune System

Molecular Motors

Drug Development

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