Question 1

Which of these are commonly used to cleave peptide bonds in polypeptides?

Accepted Answer

A)  2-mercaptoethanol ( β\betaβ -M
E)  
B)  dansyl chloride
C)  iodoacetate
D)  sodium dodecyl sulfate
E)  trypsin F) B) and E)
G) None of the above

Question 2

Hydrophobic interaction chromatography can be used to separate proteins based on differences in

Accepted Answer

A)  ionic charge.
B)  solubility.
C)  size.
D)  polarity.
E)  binding specificity.F) A) and B)
G) B) and E)

Question 3

The acronym HPLC stands for

Accepted Answer

A)  hydrophobic protein liquid chromatography.
B)  high performance liquid chromatography.
C)  hydrophilic partition liquid chromatography.
D)  high priced liquid chromatography.
E)  hydrostatic process liquid chromatography.F) C) and D)
G) A) and E)

Question 4

Matching

-In order for DEAE to act as an anion exchanger,it must have a ______.

Accepted Answer

A)   electrophoresis
B)   hydrophobic interaction
C)   enzyme-linked immunosorbent assay
D)   three-dimensional shape
E)   N-terminal amino acidF)  negative chargeG)  nucleasesH)  chromophoreI)  foaming J)  high level expressionK)  2-mercaptoethanolL)  positive chargeM)  cation exchangeN)  pIO)  chymotrypsinP)  C-terminal amino acidQ)  Sodium dodecyl sulfateR) G) and J)
S) B) and E)

Question 5

The pK1,pK2,and pKR of the amino acid histdine are 1.8,9.3,and 6.0,respectively.The pK1,pK2,and pKR of the amino acid arginine are 1.8,9.0,and 12.5,respectively.You have a mixture of histidine and arginine,how would you try to separate these two amino acids?

Accepted Answer

A)  anion exchange chromatography at pH 2
B)  anion exchange chromatography at pH 4
C)  cation exchange chromatography at pH 2
D)  cation exchange chromatography at pH 4
E)  cation exchange chromatography at pH 9F) B) and E)
G) D) and E)

Question 6

SDS-PAGE separates proteins primarily due to differences in

Accepted Answer

A)  isoelectric point.
B)  mass.
C)  polarity.
D)  solubility.
E)  amino acid sequence.F) A) and E)
G) B) and E)

Question 7

______________ has emerged as a technique for protein sequencing.

Accepted Answer

A)  NMR spectroscopy
B)  Mass spectrometry
C)  Gel electrophoresis
D)  Phylogenetic analysis
E)  Limited proteolysisF) B) and D)
G) C) and D)

Question 8

A first step in purifying a protein that was initially associated with fatty substances would be

Accepted Answer

A)  Coomassie Brilliant Blue dye staining.
B)  analytical ultracentrifugation.
C)  ELISA.
D)  Western blotting.
E)  hydrophobic interaction chromatography.F) B) and E)
G) B) and D)

Question 9

Matching

-Molecules that contain a(n) ______ are capable of absorbing light.

Accepted Answer

A)   electrophoresis
B)   hydrophobic interaction
C)   enzyme-linked immunosorbent assay
D)   three-dimensional shape
E)   N-terminal amino acidF)  negative chargeG)  nucleasesH)  chromophoreI)  foaming J)  high level expressionK)  2-mercaptoethanolL)  positive chargeM)  cation exchangeN)  pIO)  chymotrypsinP)  C-terminal amino acidQ)  Sodium dodecyl sulfateR) M) and P)
S) G) and K)

Question 10

Matching

-The endoprotease ______ cleaves polypeptides on the C-terminal side of certain bulky hydrophobic amino acid residues.

Accepted Answer

A)   electrophoresis
B)   hydrophobic interaction
C)   enzyme-linked immunosorbent assay
D)   three-dimensional shape
E)   N-terminal amino acidF)  negative chargeG)  nucleasesH)  chromophoreI)  foaming J)  high level expressionK)  2-mercaptoethanolL)  positive chargeM)  cation exchangeN)  pIO)  chymotrypsinP)  C-terminal amino acidQ)  Sodium dodecyl sulfateR) C) and H)
S) B) and L)

Question 11

Paralogous genes are

Accepted Answer

A)  genes that do not encode protein.
B)  genes of slowly evolving proteins.
C)  relics of genes that are not expressed.
D)  genes of rapidly evolving proteins.
E)  the results of gene duplication.F) D) and E)
G) C) and D)

Question 12

The quantitation of proteins due to their absorbance at ~280 nm (UV region) is due to the large absorbtivity of the ________ amino acids.

Accepted Answer

A)  anionic
B)  dansylated
C)  cleaved
D)  polar
E)  aromaticF) A) and B)
G) A) and E)

Question 13

Which physical characteristic is not commonly used in protein separation?

Accepted Answer

A)  solubility
B)  stereochemistry
C)  size
D)  charge
E)  polarityF) A) and B)
G) A) and C)

Question 14

Which of the following amino acids would be last to elute at pH 8.0 from an anion-exchange column?

Accepted Answer

A)  lysine
B)  alanine
C)  glutamic acid
D)  asparagine
E)  glycineF) B) and C)
G) C) and E)

Question 15

Natural proteins most commonly contain linear polypeptides between 100 and 1000 residues in length.One of the reasons polypeptides outside this range may be disfavored is that

Accepted Answer

A)  larger polypeptides would likely be insoluble.
B)  smaller polypeptides do not form stable folded structures.
C)  smaller polypeptides typically assemble into prion-like aggregates.
D)  amide linkages are not strong enough to keep larger polypeptides intact.
E)  ribosomes are unable to synthesize larger polypeptides.F) A) and B)
G) B) and E)

Question 16

You are interested in receptor protein-tyrosine kinases and you are purifying a novel phosphotyrosine-binding protein (NPBP-1).In order to characterize this protein you need to separate it from three other proteins (X,Y,and Z)that are still present in your partially purified material.The proteins in your preparation have the following properties:
  
a.What type of separation technique can be used to separate protein NPBP-1 from protein X?
b.What type of separation technique can be used to separate protein NPBP-1 from protein Y?
c.What type of separation technique can be used to separate protein NPBP-1 from protein Z?

Accepted Answer

a.On a size (mass)basis:gel permeation c...

Question 17

Which of these reagents is commonly used to determine the number of polypeptides in a protein?

Accepted Answer

A)  iodoacetate
B)  dansyl chloride
C)  2-mercaptoethanol ( β\betaβ -M
E)  
D)  cyanogen bromide
E)  DEAE F) A) and D)
G) A) and B)

Question 18

Matching

-If antibodies to the protein being assayed are available,a(n) ______ can be carried out.

Accepted Answer

A)   electrophoresis
B)   hydrophobic interaction
C)   enzyme-linked immunosorbent assay
D)   three-dimensional shape
E)   N-terminal amino acidF)  negative chargeG)  nucleasesH)  chromophoreI)  foaming J)  high level expressionK)  2-mercaptoethanolL)  positive chargeM)  cation exchangeN)  pIO)  chymotrypsinP)  C-terminal amino acidQ)  Sodium dodecyl sulfateR) B) and I)
S) H) and L)

Question 19

Matching

-If the cDNA for a protein has been cloned,it may be possible to obtain large quantities of the protein by _________________ in bacteria.

Accepted Answer

A)   electrophoresis
B)   hydrophobic interaction
C)   enzyme-linked immunosorbent assay
D)   three-dimensional shape
E)   N-terminal amino acidF)  negative chargeG)  nucleasesH)  chromophoreI)  foaming J)  high level expressionK)  2-mercaptoethanolL)  positive chargeM)  cation exchangeN)  pIO)  chymotrypsinP)  C-terminal amino acidQ)  Sodium dodecyl sulfateR) H) and M)
S) A) and C)

Question 20

What can be done to increase the rate at which a protein of interest moves down an ion-exchange chromatography column?

Accepted Answer

A)  reduce the ion concentration in the eluant
B)  add a small amount of a non-ionic detergents to the eluant
C)  change the pH of the eluant
D)  add a protease inhibitor to the eluant
E)  reduce the temperature of the eluantF) A) and E)
G) A) and B)

Exam 5: Proteins: Primary Structure

Paralogous genes are

Correct Answer
verified

Which of the following amino acids would be last to elute at pH 8.0 from an anion-exchange column?

Correct Answer
verified

Hydrophobic interaction chromatography can be used to separate proteins based on differences in

Correct Answer
verified

What can be done to increase the rate at which a protein of interest moves down an ion-exchange chromatography column?

Correct Answer
verified

Matching -The endoprotease ______ cleaves polypeptides on the C-terminal side of certain bulky hydrophobic amino acid residues.

Correct Answer
verified

The acronym HPLC stands for

Correct Answer
verified

The quantitation of proteins due to their absorbance at ~280 nm (UV region) is due to the large absorbtivity of the ________ amino acids.

Correct Answer
verified

Which of these reagents is commonly used to determine the number of polypeptides in a protein?

Correct Answer
verified

Matching -If the cDNA for a protein has been cloned,it may be possible to obtain large quantities of the protein by _________________ in bacteria.

Correct Answer
verified

______________ has emerged as a technique for protein sequencing.

Correct Answer
verified

Correct Answer
verified
a.On a size (mass)basis:gel permeation c...
View Answer

Matching -In order for DEAE to act as an anion exchanger,it must have a ______.

Correct Answer
verified

SDS-PAGE separates proteins primarily due to differences in

Correct Answer
verified

Matching -If antibodies to the protein being assayed are available,a(n) ______ can be carried out.

Correct Answer
verified

Natural proteins most commonly contain linear polypeptides between 100 and 1000 residues in length.One of the reasons polypeptides outside this range may be disfavored is that

Correct Answer
verified

Which physical characteristic is not commonly used in protein separation?

Correct Answer
verified

Matching -Molecules that contain a(n) ______ are capable of absorbing light.

Correct Answer
verified

Which of these are commonly used to cleave peptide bonds in polypeptides?

Correct Answer
verified

The pK₁,pK₂,and pK_R of the amino acid histdine are 1.8,9.3,and 6.0,respectively.The pK₁,pK₂,and pK_R of the amino acid arginine are 1.8,9.0,and 12.5,respectively.You have a mixture of histidine and arginine,how would you try to separate these two amino acids?

Correct Answer
verified

A first step in purifying a protein that was initially associated with fatty substances would be

Correct Answer
verified

Exam 5: Proteins: Primary Structure

Paralogous genes are

Correct AnswerverifiedShow Answer

Which of the following amino acids would be last to elute at pH 8.0 from an anion-exchange column?

Correct AnswerverifiedShow Answer

Hydrophobic interaction chromatography can be used to separate proteins based on differences in

Correct AnswerverifiedShow Answer

What can be done to increase the rate at which a protein of interest moves down an ion-exchange chromatography column?

Correct AnswerverifiedShow Answer

Matching -The endoprotease ______ cleaves polypeptides on the C-terminal side of certain bulky hydrophobic amino acid residues.

Correct AnswerverifiedShow Answer

The acronym HPLC stands for

Correct AnswerverifiedShow Answer

The quantitation of proteins due to their absorbance at ~280 nm (UV region) is due to the large absorbtivity of the ________ amino acids.

Correct AnswerverifiedShow Answer

Which of these reagents is commonly used to determine the number of polypeptides in a protein?

Correct AnswerverifiedShow Answer

Matching -If the cDNA for a protein has been cloned,it may be possible to obtain large quantities of the protein by _________________ in bacteria.

Correct AnswerverifiedShow Answer

______________ has emerged as a technique for protein sequencing.

Correct AnswerverifiedShow Answer

Correct Answerverifieda.On a size (mass)basis:gel permeation c...View AnswerShow Answer

Matching -In order for DEAE to act as an anion exchanger,it must have a ______.

Correct AnswerverifiedShow Answer

SDS-PAGE separates proteins primarily due to differences in

Correct AnswerverifiedShow Answer

Matching -If antibodies to the protein being assayed are available,a(n) ______ can be carried out.

Correct AnswerverifiedShow Answer

Natural proteins most commonly contain linear polypeptides between 100 and 1000 residues in length.One of the reasons polypeptides outside this range may be disfavored is that

Correct AnswerverifiedShow Answer

Which physical characteristic is not commonly used in protein separation?

Correct AnswerverifiedShow Answer

Matching -Molecules that contain a(n) ______ are capable of absorbing light.

Correct AnswerverifiedShow Answer

Which of these are commonly used to cleave peptide bonds in polypeptides?

Correct AnswerverifiedShow Answer

The pK1,pK2,and pKR of the amino acid histdine are 1.8,9.3,and 6.0,respectively.The pK1,pK2,and pKR of the amino acid arginine are 1.8,9.0,and 12.5,respectively.You have a mixture of histidine and arginine,how would you try to separate these two amino acids?

Correct AnswerverifiedShow Answer

A first step in purifying a protein that was initially associated with fatty substances would be

Correct AnswerverifiedShow Answer

Correct Answer
verified

Correct Answer
verified

Correct Answer
verified

Correct Answer
verified

Correct Answer
verified

Correct Answer
verified

Correct Answer
verified

Correct Answer
verified

Correct Answer
verified

Correct Answer
verified

Correct Answer
verified
a.On a size (mass)basis:gel permeation c...
View Answer

Correct Answer
verified

Correct Answer
verified

Correct Answer
verified

Correct Answer
verified

Correct Answer
verified

Correct Answer
verified

Correct Answer
verified

The pK₁,pK₂,and pK_R of the amino acid histdine are 1.8,9.3,and 6.0,respectively.The pK₁,pK₂,and pK_R of the amino acid arginine are 1.8,9.0,and 12.5,respectively.You have a mixture of histidine and arginine,how would you try to separate these two amino acids?

Correct Answer
verified

Correct Answer
verified