BICH 410 QUIZ 5 QUESTIONS ANSWERED CORRECTLY LATEST UPDATE 2026
Which of the following has the most dramatic influence on the characteristics of an individual
protein? - Answers The amino acid sequence
Which statement about insulin is correct? - Answers Insulin is composed of two polypeptides, the A
chain and the B chain.
Insulin contains an intrachain disulfide bond.
Insulin contains interchain disulfide bonds.
The A chain and the B chain of insulin are encoded by a single gene.
One of the keys to deciphering the function of a given protein is to understand its structure. - Answers
True
Only a tiny fraction of all possible proteins exist (i.e. of all combinations of protein sequence possible,
evolution has produced only a tiny fraction of the theoretical possibilities). - Answers True
An enzyme-linked immunosorbent assay requires - Answers an antibody that binds the protein of
interest.
In gel filtration chromatography, molecules are separated according to their size and shape where
larger molecules elute first and smaller molecules elute last. - Answers True
Ion-exchange chromatography - Answers Separation on the basis of charge.
Hydrophobic interaction chromatography - Answers Separation on the basis of polarity.
In two-dimensional (2D) gel electrophoresis, a sample of proteins is first subjected to isoelectric
focusing, and then to SDS-PAGE in a perpendicular direction. - Answers True
Which of these are commonly used to cleave peptide bonds in polypeptides? - Answers trypsin
Edman degradation can be used to - Answers identify the N-terminal amino acid of a polypeptide.
You have purified a new peptide hormone. To determine its amino acid sequence you have digested
the polypeptide with trypsin and in a separate reaction you have cleaved the polypeptide with
cyanogen bromide.Cleavage with trypsin yielded 5 peptides that were sequenced by Edman
degradation as shown in the following.
1. Ser-Leu
2. Asp-Val-Arg
3. Val-Met-Glu-Lys
4. Ser-Gln-Met-His-Lys
5. Ile-Phe-Met-Leu-Cys-Arg
Cleavage with cyanogen bromide yielded 4 peptides that were sequenced by Edman degradation:
1. His-Lys-Ser-Leu
2. Asp-Val-Arg-Val-Met
3. Glu-Lys-Ile-Phe-Met
4. Leu-Cys-Arg-Ser-Gln-Met
Determine the identity of the N-terminal amino acid after reconstructing the intact protein. - Answers
Asp
Which reagent reduces disulfide bonds to sulfhydryl groups? - Answers 2-mercaptoethanol
In protein sequencing, the protein is typically degraded into smaller peptides which are sequenced
and the full-length protein sequence is then reconstructed by assembling the overlapping fragments. -
Answers True
The _____ structure of a protein is the amino acid sequence of its polypeptide chain, or chains if the
protein consists of more than one polypeptide. - Answers primary
Only a tiny fraction of all possible proteins exist (i.e. of all combinations of protein sequence possible,
evolution has produced only a tiny fraction of the theoretical possibilities). - Answers True
Ion-exchange chromatography - Answers Separation on the basis of charge.
Hydrophobic interaction chromatography - Answers Separation on the basis of polarity.
Gel filtration chromatography - Answers Separation on the basis of size and shape.
Affinity chromatography - Answers Separation on the basis of binding specificity.
_____ is commonly used for salting out proteins because of its high solubility in water. - Answers
ammonium sulfate
In polyacrylamide gel electrophoresis, ________ is often used to denature the proteins and facilitate
protein separation through gel filtration effects. - Answers sds
______ uses a stable pH gradient to separate proteins. - Answers isoelectric focusing
Which of the following has the most dramatic influence on the characteristics of an individual
protein? - Answers The amino acid sequence
Which statement about insulin is correct? - Answers Insulin is composed of two polypeptides, the A
chain and the B chain.
Insulin contains an intrachain disulfide bond.
Insulin contains interchain disulfide bonds.
The A chain and the B chain of insulin are encoded by a single gene.
One of the keys to deciphering the function of a given protein is to understand its structure. - Answers
True
Only a tiny fraction of all possible proteins exist (i.e. of all combinations of protein sequence possible,
evolution has produced only a tiny fraction of the theoretical possibilities). - Answers True
An enzyme-linked immunosorbent assay requires - Answers an antibody that binds the protein of
interest.
In gel filtration chromatography, molecules are separated according to their size and shape where
larger molecules elute first and smaller molecules elute last. - Answers True
Ion-exchange chromatography - Answers Separation on the basis of charge.
Hydrophobic interaction chromatography - Answers Separation on the basis of polarity.
In two-dimensional (2D) gel electrophoresis, a sample of proteins is first subjected to isoelectric
focusing, and then to SDS-PAGE in a perpendicular direction. - Answers True
Which of these are commonly used to cleave peptide bonds in polypeptides? - Answers trypsin
Edman degradation can be used to - Answers identify the N-terminal amino acid of a polypeptide.
You have purified a new peptide hormone. To determine its amino acid sequence you have digested
the polypeptide with trypsin and in a separate reaction you have cleaved the polypeptide with
cyanogen bromide.Cleavage with trypsin yielded 5 peptides that were sequenced by Edman
degradation as shown in the following.
1. Ser-Leu
2. Asp-Val-Arg
3. Val-Met-Glu-Lys
4. Ser-Gln-Met-His-Lys
5. Ile-Phe-Met-Leu-Cys-Arg
Cleavage with cyanogen bromide yielded 4 peptides that were sequenced by Edman degradation:
1. His-Lys-Ser-Leu
2. Asp-Val-Arg-Val-Met
3. Glu-Lys-Ile-Phe-Met
4. Leu-Cys-Arg-Ser-Gln-Met
Determine the identity of the N-terminal amino acid after reconstructing the intact protein. - Answers
Asp
Which reagent reduces disulfide bonds to sulfhydryl groups? - Answers 2-mercaptoethanol
In protein sequencing, the protein is typically degraded into smaller peptides which are sequenced
and the full-length protein sequence is then reconstructed by assembling the overlapping fragments. -
Answers True
The _____ structure of a protein is the amino acid sequence of its polypeptide chain, or chains if the
protein consists of more than one polypeptide. - Answers primary
Only a tiny fraction of all possible proteins exist (i.e. of all combinations of protein sequence possible,
evolution has produced only a tiny fraction of the theoretical possibilities). - Answers True
Ion-exchange chromatography - Answers Separation on the basis of charge.
Hydrophobic interaction chromatography - Answers Separation on the basis of polarity.
Gel filtration chromatography - Answers Separation on the basis of size and shape.
Affinity chromatography - Answers Separation on the basis of binding specificity.
_____ is commonly used for salting out proteins because of its high solubility in water. - Answers
ammonium sulfate
In polyacrylamide gel electrophoresis, ________ is often used to denature the proteins and facilitate
protein separation through gel filtration effects. - Answers sds
______ uses a stable pH gradient to separate proteins. - Answers isoelectric focusing
