P. Solubility is often manipulated through iii. Salting out, a method that alters solubility to precipitate proteins.
Q. Ionic charge is the basis for iv. Isoelectric focusing, where proteins are separated based on their charge at different pH levels.
R. Polarity influences interactions in i. Reverse phase chromatography, which separates molecules based on their hydrophobicity or hydrophilicity. S. Molecular size is a primary factor in ii. Ultracentrifugation, which separates particles based on size and density. Conclusion:
These matches highlight the specific properties that influence the separation techniques, providing a clear connection between molecular characteristics and biochemical methodologies.
Match the techniques in Group I with their applications in Group II for protein analysis
Group I Group II
(P) Nuclear magnetic resonance spectroscopy (1) Proximity between specific sites
(Q) Fluorescence resonance energy transfer (2) Concentration
(R) Ultraviolet absorption spectroscopy (3) Size
(S) Dynamic light scattering (4) Structure