Question 1

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 2

How can the mass of an unknown protein can be determined using gel electrophoresis?

Accepted Answer

The mass of an unknown protein can be de

Question 3

Analyze and interpret the 2-D PAGE gel shown below.What information can be determined about the proteins labeled A and B?

Accepted Answer

Protein A has a higher mass an

Question 4

In solid-phase peptide synthesis,which reagent is used to remove the peptide from the solid resin support?

Accepted Answer

A)  HF 
B)  DCC 
C)  Fmoc 
D)  PITC 
A)  HF 
B)  DCC 
C)  Fmoc 
D)  PITC

Question 5

One of the most difficult steps in X-ray crystallography is

Accepted Answer

A)  using the correct radio frequency pulses to perturb the nuclear spin. 
B)  determining the phases of diffracted X-rays. 
C)  dissolving the protein in the appropriate solvent. 
D)  obtaining a large enough sample for analysis. 
A)  using the correct radio frequency pulses to perturb the nuclear spin. 
B)  determining the phases of diffracted X-rays. 
C)  dissolving the protein in the appropriate solvent. 
D)  obtaining a large enough sample for analysis.

Question 6

When preparing to isolate proteins from plant cells,the first step in preparing the cell homogenate would be

Accepted Answer

A)  sonication. 
B)  using a French press. 
C)  treatment with mild detergents. 
D)  enzymatic treatment. 
A)  sonication. 
B)  using a French press. 
C)  treatment with mild detergents. 
D)  enzymatic treatment.

Question 7

Which of the following peptides would be eluted last when separated using gel filtration chromatography?

Accepted Answer

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

Question 8

During solid-phase peptide synthesis,9-fluorenylmethoxycarbonyl is used

Accepted Answer

A)  as a blocking agent. 
B)  as an activating agent. 
C)  to cleave the peptide from the resin. 
D)  to couple amino acids during the synthesis. 
A)  as a blocking agent. 
B)  as an activating agent. 
C)  to cleave the peptide from the resin. 
D)  to couple amino acids during the synthesis.

Question 9

The figure below shows three proteins that are separated using gel filtration chromatography.Which protein is the largest?

Accepted Answer

A)  squares 
B)  circles 
C)  triangles 
D)  Not enough information is included to determine the protein. 
A)  squares 
B)  circles 
C)  triangles 
D)  Not enough information is included to determine the protein.

Question 10

The step in solid-phase peptide synthesis that occurs at number 2 is

Accepted Answer

A)  deblocking of the residue attached to the resin. 
B)  coupling of the amino acid. 
C)  cleavage from the resin. 
D)  activation of the Fmoc blocked residue. 
A)  deblocking of the residue attached to the resin. 
B)  coupling of the amino acid. 
C)  cleavage from the resin. 
D)  activation of the Fmoc blocked residue.

Question 11

Protein NMR is more useful than X-ray crystallography for studying

Accepted Answer

A)  secondary structure elements. 
B)  large proteins. 
C)  protein unfolding. 
D)  static protein structures. 
A)  secondary structure elements. 
B)  large proteins. 
C)  protein unfolding. 
D)  static protein structures.

Question 12

In isoelectric focusing,

Accepted Answer

A)  positively charged proteins migrate toward the cathode. 
B)  positively charged proteins migrate toward the anode. 
C)  small proteins migrate the fastest. 
D)  large proteins migrate the fastest. 
A)  positively charged proteins migrate toward the cathode. 
B)  positively charged proteins migrate toward the anode. 
C)  small proteins migrate the fastest. 
D)  large proteins migrate the fastest.

Question 13

The majority of serum proteins and nonspecific antibodies are removed during the generation of polyclonal antibodies by

Accepted Answer

A)  washing with a low pH buffer. 
B)  gel electrophoresis. 
C)  size exclusion chromatography. 
D)  salting out. 
A)  washing with a low pH buffer. 
B)  gel electrophoresis. 
C)  size exclusion chromatography. 
D)  salting out.

Question 14

How does NMR spectroscopy differ from X-ray crystallography when determining the structure of a protein?

Accepted Answer

X-ray crystallography gives the atomic p

Question 15

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 16

How does the directionality of synthesis differ with in vivo polypeptide synthesis compared to solid-phase peptide synthesis?

Accepted Answer

In in vivo polypeptide synthesis,amino a

Question 17

After centrifugation,there is a 10% decrease in activity and a 75% decrease in total protein.What is purification of the target protein?

Accepted Answer

A)  0.28-fold 
B)  1.3-fold 
C)  3.6-fold 
D)  7.5-fold 
A)  0.28-fold 
B)  1.3-fold 
C)  3.6-fold 
D)  7.5-fold

Question 18

What is the advantage of using sodium dodecyl sulfate (SDS)in gel electrophoresis?

Accepted Answer

Gel electrophoresis separates molecules

Exam 5: Methods in Protein Biochemistry

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

How can the mass of an unknown protein can be determined using gel electrophoresis?

Analyze and interpret the 2-D PAGE gel shown below.What information can be determined about the proteins labeled A and B?

In solid-phase peptide synthesis,which reagent is used to remove the peptide from the solid resin support?

One of the most difficult steps in X-ray crystallography is

When preparing to isolate proteins from plant cells,the first step in preparing the cell homogenate would be

Which of the following peptides would be eluted last when separated using gel filtration chromatography?

During solid-phase peptide synthesis,9-fluorenylmethoxycarbonyl is used

The figure below shows three proteins that are separated using gel filtration chromatography.Which protein is the largest?

The step in solid-phase peptide synthesis that occurs at number 2 is

Protein NMR is more useful than X-ray crystallography for studying

In isoelectric focusing,

The majority of serum proteins and nonspecific antibodies are removed during the generation of polyclonal antibodies by

How does NMR spectroscopy differ from X-ray crystallography when determining the structure of a protein?

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

How does the directionality of synthesis differ with in vivo polypeptide synthesis compared to solid-phase peptide synthesis?

After centrifugation,there is a 10% decrease in activity and a 75% decrease in total protein.What is purification of the target protein?

What is the advantage of using sodium dodecyl sulfate (SDS)in gel electrophoresis?

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