Question 1

The mobility of proteins in SDS-PAGE is inversely proportional to the _____________.

Accepted Answer

logarithm of their mass OR log of their molecular weight

Question 2

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 C

Question 3

What is the advantage of adding SDS to gel electrophoresis?

Accepted Answer

A)  SDS colors the proteins for visualization. 
B)  SDS reduces disulfide bonds. 
C)  SDS allows proteins to be separated on the basis of approximate mass. 
D)  None of the answers is correct. 
E)  All of the answers are correct. 
A)  SDS colors the proteins for visualization. 
B)  SDS reduces disulfide bonds. 
C)  SDS allows proteins to be separated on the basis of approximate mass. 
D)  None of the answers is correct. 
E)  All of the answers are correct. C

Question 4

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 5

Proteins can be separated from small molecules and ions through a semipermeable membrane by __________________.

Accepted Answer

The answer of Proteins can be separated from small molecules...

Question 6

What type of information can be obtained from ultracentrifugation?

Accepted Answer

This technique can be used to

Question 7

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,which...

Question 8

Which of the following is often the first step in protein purification from a homogenate?

Accepted Answer

A)  ion exchange chromatography 
B)  gel-filtration chromatography 
C)  HPLC 
D)  centrifugation 
E)  gel electrophoresis 
A)  ion exchange chromatography 
B)  gel-filtration chromatography 
C)  HPLC 
D)  centrifugation 
E)  gel electrophoresis

Question 9

Which type of protein purification relies on the attraction of the protein for a particular chemical group?

Accepted Answer

A)  affinity chromatography 
B)  gel-filtration chromatography 
C)  HPLC 
D)  gel electrophoresis 
E)  isoelectric focusing 
A)  affinity chromatography 
B)  gel-filtration chromatography 
C)  HPLC 
D)  gel electrophoresis 
E)  isoelectric focusing

Question 10

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

Accepted Answer

A)  mass 
B)  shape 
C)  the density of the solution 
D)  All of the answers are correct. 
E)  mass and shape 
A)  mass 
B)  shape 
C)  the density of the solution 
D)  All of the answers are correct. 
E)  mass and shape

Question 11

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 12

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 13

How is lactate dehydrogenase assayed?

Accepted Answer

It is assayed by the increase

Question 14

Which technique cannot be used for quantitative analysis?

Accepted Answer

A)  x-ray crystallography 
B)  ELISA 
C)  absorbance spectroscopy 
D)  All of the answers are correct. 
E)  None of the answers is correct. 
A)  x-ray crystallography 
B)  ELISA 
C)  absorbance spectroscopy 
D)  All of the answers are correct. 
E)  None of the answers is correct.

Question 15

Describe the Edman degradation method for protein-sequence analysis.

Accepted Answer

A pure protein is reacted with phenyl is

Question 16

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

Accepted Answer

Although both are used in purification,t

Question 17

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 18

When enzymes are purified,the assay is often based on

Accepted Answer

A)  light absorbance. 
B)  catalytic activity. 
C)  pH. 
D)  temperature changes. 
E)  mRNA levels. 
A)  light absorbance. 
B)  catalytic activity. 
C)  pH. 
D)  temperature changes. 
E)  mRNA levels.

Question 19

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 20

What are some of the advantages and drawbacks of NMR spectroscopy compared to x-ray crystallography?

Accepted Answer

While both are expensive and time-consum

Exam 3: Exploring Proteins and Proteomes

The mobility of proteins in SDS-PAGE is inversely proportional to the _____________.

Which of the following are used to sequence entire proteins?

What is the advantage of adding SDS to gel electrophoresis?

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

Proteins can be separated from small molecules and ions through a semipermeable membrane by __________________.

What type of information can be obtained from ultracentrifugation?

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.

Which of the following is often the first step in protein purification from a homogenate?

Which type of protein purification relies on the attraction of the protein for a particular chemical group?

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

Proteins that are not catalysts are often probed or assayed using

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

How is lactate dehydrogenase assayed?

Which technique cannot be used for quantitative analysis?

Describe the Edman degradation method for protein-sequence analysis.

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

Protein databases

When enzymes are purified,the assay is often based on

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

What are some of the advantages and drawbacks of NMR spectroscopy compared to x-ray crystallography?

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

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

Oxidative Phosphorylation

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

Filters