Question 1

Edman degradation will:

Accepted Answer

A)  determine the C-terminal amino acid by using a carboxypeptidase. 
B)  cleave the protein into a multitude of smaller peptides. 
C)  compare overlapping sets of peptide fragments. 
D)  determine the N-terminal amino acid. 
E)  generate two different, but overlapping sets of peptide fragments. 
A)  determine the C-terminal amino acid by using a carboxypeptidase. 
B)  cleave the protein into a multitude of smaller peptides. 
C)  compare overlapping sets of peptide fragments. 
D)  determine the N-terminal amino acid. 
E)  generate two different, but overlapping sets of peptide fragments.

Question 2

The preponderance of protein sequence information is now derived from:

Accepted Answer

A)  chemical sequencing (Edman method). 
B)  mass spectrometry. 
C)  mass spectrometry-mass spectrometry. 
D)  translating the nucleotide sequence of genes into codons, and thus amino acid sequence. 
E)  none of the above. 
A)  chemical sequencing (Edman method). 
B)  mass spectrometry. 
C)  mass spectrometry-mass spectrometry. 
D)  translating the nucleotide sequence of genes into codons, and thus amino acid sequence. 
E)  none of the above.

Question 3

The amino acid sequence is defined as ____ structure.

Accepted Answer

A)  primary 
B)  secondary 
C)  tertiary 
D)  quaternary 
E)  all are true 
A)  primary 
B)  secondary 
C)  tertiary 
D)  quaternary 
E)  all are true

Question 4

Hemoglobin is an example of a(n):

Accepted Answer

A)  enzyme. 
B)  regulatory protein. 
C)  transport protein. 
D)  storage protein. 
E)  structural protein. 
A)  enzyme. 
B)  regulatory protein. 
C)  transport protein. 
D)  storage protein. 
E)  structural protein.

Question 5

Reaction of the peptide, ala-met-lys-ser, with phenylisothiocyanate (PITC) at pH 8.0 followed by mild acidification (first cycle of Edman method) would release:

Accepted Answer

A)  the labeled peptide ala-met-lys-ser-PTH. 
B)  PTH-ala, PTH-ser, PTH-lys and PTH-met. 
C)  PTH-ser and the peptide ala-met-lys. 
D)  PTH-ala and the peptide met-lys-ser. 
E)  All of the above. 
A)  the labeled peptide ala-met-lys-ser-PTH. 
B)  PTH-ala, PTH-ser, PTH-lys and PTH-met. 
C)  PTH-ser and the peptide ala-met-lys. 
D)  PTH-ala and the peptide met-lys-ser. 
E)  All of the above.

Question 6

Hemoglobin is an α2, β2 ____ whereas, glutamine synthetase from E. coli is an α12 ____.

Accepted Answer

A)  -homodimer, -homomultimer 
B)  -heteromultimer, -homomultimer 
C)  -homomultimer, -heterodimer 
D)  -heterodimer, -monomeric protein 
E)  -heterodimer, -homomultimer 
A)  -homodimer, -homomultimer 
B)  -heteromultimer, -homomultimer 
C)  -homomultimer, -heterodimer 
D)  -heterodimer, -monomeric protein 
E)  -heterodimer, -homomultimer

Question 7

Which of the following is not a commonly used technique for protein isolation and purification?

Accepted Answer

A)  gas-liquid chromatography. 
B)  ion exchange chromatography. 
C)  electrophoresis. 
D)  solubility ("salting in" and "salting out"). 
E)  affinity chromatography. 
A)  gas-liquid chromatography. 
B)  ion exchange chromatography. 
C)  electrophoresis. 
D)  solubility ("salting in" and "salting out"). 
E)  affinity chromatography.

Question 8

Proteins destined for an extracellular location are characteristically:

Accepted Answer

A)  phosphoproteins. 
B)  glycoproteins. 
C)  lipoproteins. 
D)  nucleoproteins. 
E)  flavoproteins. 
A)  phosphoproteins. 
B)  glycoproteins. 
C)  lipoproteins. 
D)  nucleoproteins. 
E)  flavoproteins.

Question 9

All of the information necessary for a protein to achieve its intricate architecture is contained within its ____ structure.

Accepted Answer

A)  primary 
B)  secondary 
C)  tertiary 
D)  quaternary 
E)  all are true 
A)  primary 
B)  secondary 
C)  tertiary 
D)  quaternary 
E)  all are true

Question 10

Which of the following amino acids occurs most frequently in proteins?

Accepted Answer

A)  methionine 
B)  alanine 
C)  tryptophan 
D)  tyrosine 
E)  histidine 
A)  methionine 
B)  alanine 
C)  tryptophan 
D)  tyrosine 
E)  histidine

Question 11

Which of the following mutations would probably be least likely to impact the function of the protein?

Accepted Answer

A)  Lys to Ser 
B)  Ala to Asp 
C)  His to Pro 
D)  Val to Ile 
E)  Phe to Tyr 
A)  Lys to Ser 
B)  Ala to Asp 
C)  His to Pro 
D)  Val to Ile 
E)  Phe to Tyr

Question 12

Which of the following protease enzymes is correctly identified with its specificity?

Accepted Answer

A)  trypsin: cleaves on C-side of acidic amino acids 
B)  chymotrypsin: cleaves on C-side of aliphatic amino acids 
C)  staphylococcal protease: cleaves on C-side of acidic amino acids 
D)  clostripain: cleaves on C-side of lysine 
E)  none of the above are correct 
A)  trypsin: cleaves on C-side of acidic amino acids 
B)  chymotrypsin: cleaves on C-side of aliphatic amino acids 
C)  staphylococcal protease: cleaves on C-side of acidic amino acids 
D)  clostripain: cleaves on C-side of lysine 
E)  none of the above are correct

Question 13

Homologous proteins such as hemoglobin from different organisms do NOT:

Accepted Answer

A)  have nearly identical lengths. 
B)  share little sequence homology with other proteins with similar function (e.g., myoglobin). 
C)  share a significant degree of sequence similarity. 
D)  perform the same function in different organisms. 
E)  have sequence identity in direct correlation to the relatedness of the species from which they were derived. 
A)  have nearly identical lengths. 
B)  share little sequence homology with other proteins with similar function (e.g., myoglobin). 
C)  share a significant degree of sequence similarity. 
D)  perform the same function in different organisms. 
E)  have sequence identity in direct correlation to the relatedness of the species from which they were derived.

Question 14

Although they have very different functions, hen egg white lysozyme and ____ share similar sequence homology and similar tertiary structure.

Accepted Answer

A)  trypsin 
B)  α-lactalbumin 
C)  thrombin 
D)  hemoglobin 
E)  chymotrypsin 
A)  trypsin 
B)  α-lactalbumin 
C)  thrombin 
D)  hemoglobin 
E)  chymotrypsin

Question 15

The formation of a disulfide bond would be an example of what level of protein structure?

Accepted Answer

A)  primary 
B)  secondary 
C)  tertiary 
D)  quaternary 
E)  both c and d are correct 
A)  primary 
B)  secondary 
C)  tertiary 
D)  quaternary 
E)  both c and d are correct

Question 16

Molecules of a given protein have all EXCEPT:

Accepted Answer

A)  a fixed amino acid composition. 
B)  a defined amino acid sequence. 
C)  a sequence read from C-terminal end to N-terminal end. 
D)  an invariant molecular weight. 
E)  a nucleotide sequence from which they are encoded. 
A)  a fixed amino acid composition. 
B)  a defined amino acid sequence. 
C)  a sequence read from C-terminal end to N-terminal end. 
D)  an invariant molecular weight. 
E)  a nucleotide sequence from which they are encoded.

Question 17

Discuss the biological functions of proteins.​

Accepted Answer

Proteins fill essentially every biologic

Question 18

What is the product formed from the acid hydrolysis of a simple amide?

Accepted Answer

A)  acid & base 
B)  aldehyde & alcohol 
C)  acid & amine 
D)  ester & alcohol 
E)  amine & aldehyde 
A)  acid & base 
B)  aldehyde & alcohol 
C)  acid & amine 
D)  ester & alcohol 
E)  amine & aldehyde

Question 19

A common reaction of two cysteine residues in proteins results in the formation of ____.

Accepted Answer

A)  thioester bonds 
B)  disulfide bonds 
C)  dithiol bonds 
D)  thioether bonds 
E)  none of the above 
A)  thioester bonds 
B)  disulfide bonds 
C)  dithiol bonds 
D)  thioether bonds 
E)  none of the above

Question 20

Amino acid analysis of a protein gives:

Accepted Answer

A)  the sequence of the protein. 
B)  the number of residues of each amino acid in the protein. 
C)  the molecular weight of the protein. 
D)  the percentage or ratio of the various amino acids in the protein. 
E)  an identification of the N-terminal and C-terminal amino acids. 
A)  the sequence of the protein. 
B)  the number of residues of each amino acid in the protein. 
C)  the molecular weight of the protein. 
D)  the percentage or ratio of the various amino acids in the protein. 
E)  an identification of the N-terminal and C-terminal amino acids.

Exam 5: Proteins: Their Primary Structure and Biological Functions

Edman degradation will:

The preponderance of protein sequence information is now derived from:

The amino acid sequence is defined as ____ structure.

Hemoglobin is an example of a(n):

Reaction of the peptide, ala-met-lys-ser, with phenylisothiocyanate (PITC) at pH 8.0 followed by mild acidification (first cycle of Edman method) would release:

Hemoglobin is an α2, β2 ____ whereas, glutamine synthetase from E. coli is an α12 ____.

Which of the following is not a commonly used technique for protein isolation and purification?

Proteins destined for an extracellular location are characteristically:

All of the information necessary for a protein to achieve its intricate architecture is contained within its ____ structure.

Which of the following amino acids occurs most frequently in proteins?

Which of the following mutations would probably be least likely to impact the function of the protein?

Which of the following protease enzymes is correctly identified with its specificity?

Homologous proteins such as hemoglobin from different organisms do NOT:

Although they have very different functions, hen egg white lysozyme and ____ share similar sequence homology and similar tertiary structure.

The formation of a disulfide bond would be an example of what level of protein structure?

Molecules of a given protein have all EXCEPT:

Discuss the biological functions of proteins.​

What is the product formed from the acid hydrolysis of a simple amide?

A common reaction of two cysteine residues in proteins results in the formation of ____.

Amino acid analysis of a protein gives:

The Facts of Life: Chemistry Is the Logic of Biological Phenomena

Water: the Medium of Life

Thermodynamics of Biological Systems

Amino Acids and the Peptide Bond

Proteins: Secondary, Tertiary, and Quaternary Structure

Carbohydrates and the Glycoconjugates of Cell Surfaces

Lipids

Membranes and Membrane Transport

Nucleotides and Nucleic Acids

Structure of Nucleic Acids

Recombinant Dna, Cloning, Chimeric Genes, and Synthetic Biology

Enzymeskinetics and Specificity

Mechanisms of Enzyme Action

Enzyme Regulation

Molecular Motors

Metabolism: an Overview

Glycolysis

The Tricarboxylic Acid Cycle

Electron Transport and Oxidative Phosphorylation

Photosynthesis

Gluconeogenesis, Glycogen Metabolism, and the Pentose Phosphate Pathway

Fatty Acid Catabolism

Lipid Biosynthesis

Nitrogen Acquisition and Amino Acid Metabolism

Synthesis and Degradation of Nucleotides

Metabolic Integration and Organ Specialization

Dna Metabolism: Replication, Recombination, and Repair

Transcription and the Regulation of Gene Expression

Protein Synthesis

Completing the Protein Life Cycle: Folding, Processing, and Degradation

The Reception and Transmission of Extracellular Information

Filters

Hemoglobin is an α₂, β₂ whereas, glutamine synthetase from E. coli is an α1₂ .

Discuss the biological functions of proteins.