Question 1

Which technique cannot be used for quantitative analysis?

Accepted Answer

A)  zonal centrifugation 
B)  ELISA 
C)  enzyme assay 
D)  All of the above. 
E)  None of the above. 
A)  zonal centrifugation 
B)  ELISA 
C)  enzyme assay 
D)  All of the above. 
E)  None of the above.

Question 2

Describe five possible steps in protein purification. Start with a technique used on a complex mixture of proteins, such as a cell lysate, through a series of steps to a pure protein.

Accepted Answer

Homogenization, salting out, i

Question 3

Trypsin cleaves the peptide bond at:

Accepted Answer

A)  the carboxyl side of Arginine and Lysine residues. 
B)  the carboxyl side of Methionine residues. 
C)  the amino terminus. 
D)  None of the above. 
E)  All of the above. 
A)  the carboxyl side of Arginine and Lysine residues. 
B)  the carboxyl side of Methionine residues. 
C)  the amino terminus. 
D)  None of the above. 
E)  All of the above.

Question 4

Two-dimensional electrophoresis is a combination of which two techniques?

Accepted Answer

A)  isoelectric focusing and affinity chromatography 
B)  ion-exchange chromatography and SDS-PAGE 
C)  affinity chromatography and SDS-PAGE 
D)  isoelectric focusing and SDS-PAGE 
E)  isoelectric focusing and ion-exchange chromatography 
A)  isoelectric focusing and affinity chromatography 
B)  ion-exchange chromatography and SDS-PAGE 
C)  affinity chromatography and SDS-PAGE 
D)  isoelectric focusing and SDS-PAGE 
E)  isoelectric focusing and ion-exchange chromatography

Question 5

________________ allows the detection of small amounts of target proteins as well as the ability to determine the size of target proteins.

Accepted Answer

Western bl

Question 6

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

Accepted Answer

Using the amino acid sequence,

Question 7

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

Accepted Answer

Although both are used in purification,

Question 8

The ________________ of a protein is the pH at which its net charge is zero.

Accepted Answer

The answer of The ________________ of a protein is the...

Question 9

________________ gels are often used as the media for electrophoretic techniques such as SDS-PAGE and isoelectric focusing.

Accepted Answer

The answer of ________________ gels are often used as the...

Question 10

Why is there a need for different digestion tools when fingerprinting a protein?

Accepted Answer

To generate overlapping peptid

Question 11

Cyanogen bromide cleaves the peptide bond at:

Accepted Answer

A)  the carboxyl side of Arginine and Lysine residues. 
B)  the carboxyl side of Methionine residues. 
C)  the amino terminus. 
D)  None of the above. 
E)  All of the above. 
A)  the carboxyl side of Arginine and Lysine residues. 
B)  the carboxyl side of Methionine residues. 
C)  the amino terminus. 
D)  None of the above. 
E)  All of the above.

Question 12

Molecular exclusion gel or gel-filtration chromatography separates molecules on the basis of __________________.

Accepted Answer

The answer of Molecular exclusion gel or gel-filtration chromatography separates...

Question 13

Polypeptides can be fragmented into smaller peptides by cleavage with chymotrypsin, which hydrolyzes the peptide bond at the C-terminal side of ____, ______, and ______ residues.

Accepted Answer

phenyalani

Question 14

Describe the Edman degradation method for protein-sequence analysis.

Accepted Answer

A pure protein is reacted with phenyliso

Question 15

In the Edman procedure for peptide sequence, phenyl isothiocyanate is used to selectively derivitize the __________________ residue, which is then removed as a PTH derivative.

Accepted Answer

The answer of In the Edman procedure for peptide sequence,...

Question 16

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 above. 
E)  All of the above. 
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 above. 
E)  All of the above.

Question 17

What type of information can be obtained from gradient centrifugation?

Accepted Answer

This technique can be used to

Question 18

Use the following to answer questions 1-10:
Choose the correct answer from the list below. Not all of the answers will be used.
-____________: A protein purification technique characterized by high resolution and rapid separation.

Accepted Answer

A) HPLC 
B) specific activity 
C) MALDI-TOF mass spectrum 
D) gradient centrifugation 
E) proteome
F)SDS
G)two-dimensional electrophoresis
H)Svedberg
I)immunoglobulin
J)differential centrifugation
K)overlap peptides
L)affinity chromatography 
A) HPLC 
B) specific activity 
C) MALDI-TOF mass spectrum 
D) gradient centrifugation 
E) proteome
F)SDS
G)two-dimensional electrophoresis
H)Svedberg
I)immunoglobulin
J)differential centrifugation
K)overlap peptides
L)affinity chromatography

Question 19

Which types of molecules can serve as antigens?

Accepted Answer

A)  proteins 
B)  polysaccharides 
C)  metal ions 
D)  All of the above. 
E)  A and B 
A)  proteins 
B)  polysaccharides 
C)  metal ions 
D)  All of the above. 
E)  A and B

Question 20

How is lactic acid dehydrogenase assayed?

Accepted Answer

It is assayed by the increase

Exam 5: Techniques in Protein Biochemistry

Which technique cannot be used for quantitative analysis?

Describe five possible steps in protein purification. Start with a technique used on a complex mixture of proteins, such as a cell lysate, through a series of steps to a pure protein.

Trypsin cleaves the peptide bond at:

Two-dimensional electrophoresis is a combination of which two techniques?

________________ allows the detection of small amounts of target proteins as well as the ability to determine the size of target proteins.

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

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

The ________________ of a protein is the pH at which its net charge is zero.

________________ gels are often used as the media for electrophoretic techniques such as SDS-PAGE and isoelectric focusing.

Why is there a need for different digestion tools when fingerprinting a protein?

Cyanogen bromide cleaves the peptide bond at:

Molecular exclusion gel or gel-filtration chromatography separates molecules on the basis of __________________.

Polypeptides can be fragmented into smaller peptides by cleavage with chymotrypsin, which hydrolyzes the peptide bond at the C-terminal side of ____, ______, and ______ residues.

Describe the Edman degradation method for protein-sequence analysis.

In the Edman procedure for peptide sequence, phenyl isothiocyanate is used to selectively derivitize the __________________ residue, which is then removed as a PTH derivative.

What is the advantage of adding SDS to gel electrophoresis?

What type of information can be obtained from gradient centrifugation?

Use the following to answer questions 1-10: Choose the correct answer from the list below. Not all of the answers will be used. -____________: A protein purification technique characterized by high resolution and rapid separation.

Which types of molecules can serve as antigens?

How is lactic acid dehydrogenase assayed?

Biochemistry and the Unity of Life

Water, Weak Bonds, and the Generation of Order Out of Chaos

Amino Acids

Protein Three-Dimensional Structure

Basic Concepts of Enzyme Action

Kinetics and Regulation

Mechanisms and Inhibitors

Hemoglobin: an Allosteric Protein

Carbohydrates

Lipids

Membrane Structure and Function

Signal Transduction Pathways

Digestion: Turning a Meal Into Cellular Biochemicals

Metabolism: Basic Concepts and Design

Glycolysis

Gluconeogenesis

Preparation for the Cycle

Harvesting Electrons From the Cycle

The Electron Transport Chain

The Proton-Motive Force

The Light Reactions

The Calvin Cycle

Glycogen Degradation

Glycogen Synthesis

The Pentose Phosphate Pathway

Fatty Acid Degredation

Fatty Acid Synthesis

Lipid Synthesis

Amino Acid Degradation and the Urea Cycle

Amino Acids Synthesis

Nucleotide Metabolism

The Structure of Informational Macromolecules: Dna and Rna

DNA Replication

DNA Repair and Recombination

RNA Synthesis and Regulation in Prokaryotes

Gene Expression in Eukaryotes

RNA Processing in Eukaryotes

The Genetic Code

The Mechanism of Protein Synthesis

Recombinant Dna Techniques

Filters

Polypeptides can be fragmented into smaller peptides by cleavage with chymotrypsin, which hydrolyzes the peptide bond at the C-terminal side of , , and ____ residues.