The Question is from neet-botany biomolecules-biology , and it was created by the author Mr. NARESH KUMAR K

Question

A protein undergoes denaturation in a high urea concentration. Which of the following interactions is LEAST likely to be disrupted during this process?

Mr. NARESH KUMAR K · Accepted Answer

## CORE INFORMATION
✓ **Answer**: [D]
## CONCEPT FRAMEWORK
**Primary Concept**: Protein Denaturation
**Related Topics**:  Protein Structure, Non-covalent interactions, Peptide Bonds
**Prerequisites**: Basic understanding of protein structure (primary, secondary, tertiary, quaternary) and the different types of interactions that stabilize these structures. Understanding of denaturation.
## SOLUTION PATHWAY
**Given Information**:
    * Protein is denatured in high urea concentration.
    * We need to find the interaction LEAST likely to be disrupted.
**Method & Steps**:
    1. **Understand Denaturation**: Denaturation involves the disruption of the non-covalent interactions that maintain a protein's native 3D structure, leading to loss of function. Urea is a chaotropic agent that disrupts these interactions.
    2. **Analyze Interactions**: 
        * **Hydrophobic interactions**: These are crucial for protein folding, and urea disrupts these by interacting with the non-polar residues, making them more soluble and unfolding the protein.
        * **Hydrogen bonds**: These are essential for secondary structures (alpha helices, beta sheets), and urea can compete with these bonds, disrupting them.
        * **Ionic interactions**: These are formed between oppositely charged amino acid side chains and can be disrupted by high concentrations of ions, including those from urea.
        * **Peptide bonds**: These are covalent bonds that form the backbone of the protein, connecting amino acids. They are very strong and are not easily broken by denaturation.
    3. **Identify Least Likely Disrupted Interaction**:  Since urea disrupts non-covalent interactions, and peptide bonds are covalent, peptide bonds are least likely to be disrupted.
**Result**: Peptide bonds are the least likely to be disrupted during denaturation by urea.
 ## OPTION ANALYSIS
[A] :x: Hydrophobic interactions are significantly disrupted by urea, as urea molecules can interact with non-polar residues, disrupting their association.
[B] :x: Hydrogen bonds are also disrupted by urea, which can form its own hydrogen bonds, outcompeting intramolecular hydrogen bonds in proteins.
[C] :x: Ionic interactions are also disrupted by urea, due to the presence of ions that can compete with the ionic bonds within the protein.
[D] ✓: Peptide bonds are covalent bonds and are not easily broken during denaturation. They are strong and require harsh conditions like high temperatures or strong acids/bases to be broken. 
 ## LEARNING AIDS
**Common Mistakes**:
    1. **Confusing Covalent and Non-Covalent Bonds**: It's crucial to differentiate between strong covalent bonds and weaker non-covalent interactions. Denaturation primarily targets non-covalent bonds.
    2. **Thinking All Interactions are Equally Affected**: Not all interactions are equally susceptible to denaturation agents like urea. Some are more sensitive than others.
**Quick Tips**:
    1. **Remember the hierarchy**: Covalent bonds > Non-covalent bonds in terms of strength and resistance to denaturation.
    2. **Think of urea as a 'competitor'**: Urea competes for the non-covalent interactions within the protein, causing it to unfold.

Mr. NARESH KUMAR K · Answer

Hydrophobic interactions

Mr. NARESH KUMAR K · Answer

Hydrogen bonds

Mr. NARESH KUMAR K · Answer

Ionic interactions

Mr. NARESH KUMAR K · Answer

The correct Option is "Peptide bonds"

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