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

Question

Which chromatographic technique is BEST suited for separating proteins based on their differences in net charge at a given pH?

K SURESH KUMAR · Accepted Answer

## CORE INFORMATION
✓ **Answer**: C
## CONCEPT FRAMEWORK
 **Primary Concept**: Chromatography techniques for protein separation
 **Related Topics**: Ion exchange resins, protein isoelectric point (pI), net charge
 **Prerequisites**: Understanding of different chromatographic techniques and protein properties.
## SOLUTION PATHWAY
**Given Information**:
  The question asks for the best chromatographic technique to separate proteins based on their net charge at a given pH.
**Method & Steps**:
 1. Analyze each chromatographic technique and its separation principle.
  Reasoning: We need to identify the technique that exploits differences in protein net charge.
 2. Evaluate the suitability of each technique based on the given criterion.
  Working:
		* Size exclusion chromatography separates proteins based on their size and shape.
		* Affinity chromatography separates proteins based on their specific binding to a ligand.
		* Ion exchange chromatography separates proteins based on their net charge at a given pH.  Proteins with opposite charge to the stationary phase bind and are eluted by changing the salt concentration or pH.
		* Hydrophobic interaction chromatography separates proteins based on their hydrophobicity.
 3. Identify the technique that best fits the given criteria.
  Result: Ion exchange chromatography is the best suited technique because it directly separates proteins based on their net charge.
  Verification: The other options do not primarily utilize net charge for separation.
 ## OPTION ANALYSIS
A :x: Size exclusion chromatography separates based on size, not charge.
B :x: Affinity chromatography separates based on specific binding to a ligand, not charge.
C ✓: Ion exchange chromatography separates based on the net charge of the protein at a given pH. This makes it the best option for the given question.
D :x: Hydrophobic interaction chromatography separates based on hydrophobicity, not charge.
 ## LEARNING AIDS
 **Common Mistakes**:
  1.Confusing ion exchange chromatography with other techniques:  Understanding the fundamental principles of each technique is key to avoiding this error. 
  2.Overlooking the pH dependence: Remember that the net charge of a protein is pH-dependent. The effectiveness of ion exchange chromatography relies on this.
 **Quick Tips**:
  1.Remember the basic principles of each chromatographic technique: size exclusion (size), affinity (binding), ion exchange (charge), hydrophobic interaction (hydrophobicity).
  2.Visualize the process: Imagine how proteins with different charges would interact with a charged stationary phase in ion-exchange chromatography.

K SURESH KUMAR · Answer

Size exclusion chromatography

K SURESH KUMAR · Answer

Affinity chromatography

K SURESH KUMAR · Answer

The correct Option is "Ion exchange chromatography"

K SURESH KUMAR · Answer

Hydrophobic interaction chromatography

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