Which of the following is not associated with the folding of a protein into its native conformation?
options:
a) Molecular chaperones prevent folding intermediates from aggregating.
b) Folding of proteins is a relatively slow process as the stabilization of the molecular structure depends solely on salt bridge interactions which take time to form.
c) The major driving force for protein folding is the overall increase in solvent entropy. This increase in solvent entropy is a result of the strong interactions between water molecules that lead to the association of nonpolar side chains and subsequent collapse of the molecule into a more compact shape.
d) Hydrogen bonds contribute to the cooperativity of folding and help stabilize the native conformations of proteins.
e) All of the above are associated with the folding of a protein into its native conformation.
2 . A protein of interest needs to be separated from a mixture of proteins for amino acid sequencing. It is known that the protein of interest is highly enriched in lysine residues compared to the other proteins in the mixture. Which of the following techniques will be most effective in isolating this protein?
options:
a) gel-filtration chromatography
b) SDS-polyacrylamide gel electrophoresis
c) mass spectrometry
d) cation exchange chromatography
e) anion exchange chromatography
Which of the following is not associated with the folding of a protein into its native conformation?
options:
| a) | Molecular chaperones prevent folding intermediates from aggregating. |
| b) | Folding of proteins is a relatively slow process as the stabilization of the molecular structure depends solely on salt bridge interactions which take time to form. |
| c) | The major driving force for protein folding is the overall increase in solvent entropy. This increase in solvent entropy is a result of the strong interactions between water molecules that lead to the association of nonpolar side chains and subsequent collapse of the molecule into a more compact shape. |
| d) | Hydrogen bonds contribute to the cooperativity of folding and help stabilize the native conformations of proteins. |
| e) | All of the above are associated with the folding of a protein into its native conformation. |
2 . A protein of interest needs to be separated from a mixture of proteins for amino acid sequencing. It is known that the protein of interest is highly enriched in lysine residues compared to the other proteins in the mixture. Which of the following techniques will be most effective in isolating this protein?
options:
| a) | gel-filtration chromatography |
| b) | SDS-polyacrylamide gel electrophoresis |
| c) | mass spectrometry |
| d) | cation exchange chromatography |
| e) | anion exchange chromatography |
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