Addition of an electrolyte such as sodium dodecyl sulphate causes

Options

A. renaturation of proteins since it stabilises hydrophobic interactions
B. denaturation of proteins since it disturbs hydrophobic interactions
C. renaturation of proteins since it maintains necessary isoelectric point
D. denaturation of proteins since it cause cleavage of `O=C-N-H` bonds

Answer

To answer the question about the effect of adding an electrolyte such as sodium dodecyl sulfate (SDS), we can follow these steps:

### Step-by-Step Solution:

1. **Understanding Sodium Dodecyl Sulfate (SDS)**:
- Sodium dodecyl sulfate (SDS) is a detergent with the chemical formula CH3(CH2)11OSO3Na. It is an anionic detergent commonly used in biochemistry and molecular biology.

**Hint**: Remember that SDS is an anionic detergent, which means it carries a negative charge.

2. **Role of SDS in Protein Chemistry**:
- SDS is primarily used to denature proteins. Denaturation refers to the process where proteins lose their native structure due to the disruption of non-covalent interactions, such as hydrophobic interactions and hydrogen bonds.

**Hint**: Denaturation involves the unfolding of protein structures, leading to loss of function.

3. **Mechanism of Denaturation**:
- When SDS is added to a protein solution, it interacts with the protein molecules and disrupts the hydrophobic interactions that stabilize the protein structure. This disruption leads to the unfolding of the protein.

**Hint**: Focus on how SDS affects the hydrophobic interactions within proteins.

4. **Electrophoresis Application**:
- SDS is particularly useful in polyacrylamide gel electrophoresis (PAGE), a technique used to separate proteins based on their molecular weight. The negative charge from SDS allows proteins to migrate towards the positive electrode during electrophoresis.

**Hint**: Electrophoresis is a technique that separates molecules based on size and charge.

5. **Evaluating the Options**:
- Now, let's analyze the options given in the question:
- **Renaturation of protein since it is stabilized hydrophobic interaction**: Incorrect, as SDS denatures proteins.
- **Denaturation of protein since it disturbs hydrophobic interaction**: Correct, as this is the primary effect of SDS.
- **Renaturation of protein since it maintains necessary isoelectric point**: Incorrect, as SDS does not maintain the isoelectric point.
- **Denaturation of protein since it causes cleavage of O=C-H bond**: Incorrect, as SDS does not cleave covalent bonds but disrupts non-covalent interactions.

**Hint**: Carefully consider how each option relates to the action of SDS on proteins.

### Conclusion:
The correct answer to the question is: **Denaturation of protein since it disturbs hydrophobic interaction**.