Unit-III Methods of Studying MacromoleculesBy abdulslambsn@gmail.com / June 14, 2025 Quiz 3 | Unit-III Methods Of Studying Macromolecules Your Good Name: Your College Name: Morning/Evening/Private: Email: 1. Affinity chromatography utilizes: Molecular charge Molecular shape Specific binding between a molecule and its ligand Viscosity of a solution None 2. Which stationary phase is used in gel filtration chromatography? Agarose or polyacrylamide beads Silica gel Paper Activated charcoal None 3. Electrophoresis separates molecules based on: Color Shape Net charge and size Temperature None 4. Which type of electrophoresis does not involve a gel matrix? SDS-PAGE Agarose electrophoresis Free-boundary electrophoresis Capillary electrophoresis None 5. Which property of a macromolecule is primarily assessed by viscosity measurements? Molecular charge Molecular shape and size pH sensitivity Binding affinity None 6. Relative viscosity is calculated by comparing: pH of two solutions Absorbance values Flow time of solvent and solution Conductivity of solutions None 7. The unit of viscosity is: Pascal Poise Hertz Dalton None 8. A polymer that shows high intrinsic viscosity likely has: Low molecular mass Branched and compact structure Linear and extended structure Spherical structure None 9. In gel filtration chromatography, macromolecules are separated based on: Charge Size Polarity Affinity None 10. Which of the following will elute first in gel filtration chromatography? Small proteins Large proteins Negatively charged proteins Hydrophilic proteins None 11. In SDS-PAGE, SDS imparts what property to proteins? Positive charge Uniform negative charge Fluorescence Solubility None 12. Free-boundary electrophoresis is performed in: Agarose gel Liquid buffer without gel Polyacrylamide gel Chromatographic column None 13. Sedimentation velocity is used to study: Rate of macromolecular separation Molecular charge Color of macromolecules Heat sensitivity None 14. Sedimentation equilibrium allows determination of: Sedimentation rate only Molecular weight without shape effect Only density Electrical charge None 15. Svedberg unit (S) is the unit of: pH Viscosity Sedimentation coefficient Molecular weight None 16. A particle with a high Svedberg value is likely to be: Large and dense Small and light Negatively charged Basic in nature None 17. A researcher wants to separate proteins based on size and estimate their molecular weight. Which combination is best? SDS-PAGE and ion-exchange chromatography Gel filtration and SDS-PAGE Affinity chromatography and blotting Viscosity and affinity None 18. Which method can give an approximate molecular weight of a native protein complex in solution? SDS-PAGE Affinity chromatography Sedimentation equilibrium Paper chromatography None 19. Which method is most suitable to assess protein-ligand interaction specificity? Ion-exchange chromatography Gel filtration Affinity chromatography Electrophoresis None 20. To study shape and conformational changes in macromolecules, which method is useful? Viscosity measurement Paper chromatography Simple diffusion test Colorimetric test None 21. Which method allows monitoring the homogeneity of a macromolecular sample during centrifugation? Sedimentation velocity Gel electrophoresis Ion exchange Chromatofocusing None 22. In ion-exchange chromatography, proteins are separated based on their: Molecular weight Charge Density Shape None 23. An increase in viscosity of a solution indicates: Smaller molecular weight Presence of more solvent Larger or more elongated molecules Degradation of macromolecules None 24. The migration rate of a molecule in electrophoresis depends on all EXCEPT: Electric field strength Buffer pH Shape of the gel tank Size of the molecule None 25. The ultracentrifuge is used in: Paper chromatography Free-boundary electrophoresis Sedimentation analysis Viscosity measurement None 1 out of 3 Thanks For Submitting Your Quiz !!