Multiple Choice
By adding SDS to a protein and performing gel electrophoresis, it is possible to:
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5. Protein Techniques
SDS-PAGE
Multiple Choice
Which of the following statements are true regarding the treatment of proteins with SDS?
i) Only proteins with native net charges acquire an overall net negative charge.
ii) Proteins denature due to a disruption of the hydrophobic interactions stabilizing the core of their structures.
iii) All protein subunits can be separated via SDS-PAGE.
A
i, ii, iii.
B
i, ii.
C
ii, iii.
D
i, iii.
E
ii.
Verified step by step guidance1
Understand the role of SDS (sodium dodecyl sulfate) in protein analysis: SDS is an anionic detergent that binds to proteins, giving them a uniform negative charge and denaturing them by disrupting non-covalent bonds.
Evaluate statement i: SDS imparts a negative charge to all proteins, not just those with native net charges. Therefore, this statement is false.
Evaluate statement ii: SDS denatures proteins by disrupting hydrophobic interactions, which are crucial for maintaining the protein's tertiary structure. This statement is true.
Evaluate statement iii: SDS-PAGE separates proteins based on size, not charge or subunit composition. While SDS can separate subunits of a protein complex, it does not guarantee separation of all subunits if they are covalently linked. This statement is partially true but not universally applicable.
Conclude which statements are true: Based on the evaluations, only statement ii is consistently true regarding the treatment of proteins with SDS.
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