Biophysics of Macromolecules – MCQs 

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1. The primary structure of a protein refers to:





2. DNA double helix stability is mainly due to:





3. The α-helix is stabilized by:





4. β-sheets in proteins are stabilized by:





5. The quaternary structure of a protein refers to:





6. Protein folding is often guided by:





7. RNA secondary structures are stabilized by:





8. Which technique is most common for determining 3D structure of macromolecules?





9. Circular dichroism spectroscopy is mainly used to study:





10. The Ramachandran plot shows allowed regions of:





11. Molecular chaperones assist in:





12. Denaturation of proteins involves:





13. DNA melting temperature (Tm) increases with:





14. Nucleic acids absorb UV light strongly at:





15. Proteins absorb UV light strongly at:





16. Hydrophobic collapse in protein folding refers to:





17. The B-form of DNA is:





18. The Z-form of DNA is:





19. NMR spectroscopy is useful for studying:





20. Intrinsically disordered proteins (IDPs) are characterized by:





21. The Levinthal paradox highlights:





22. Protein aggregation is often linked to:





23. SDS in SDS-PAGE is used to:





24. Glycosidic bonds in nucleic acids link:





25. The peptide bond has partial double-bond character due to:





26. In collagen, the triple helix is stabilized by:





27. Nucleosome formation involves:





28. The hydrodynamic radius of macromolecules is measured by:





29. Single-molecule biophysics often employs:





30. The cooperative binding of oxygen to hemoglobin is explained by:





31. Protein domain refers to:





32. Hydrogen bonds in macromolecules are typically:





33. Ionic interactions in macromolecules are weakened in:





34. Hydropathy plots are used to predict:





35. Urea and guanidinium chloride denature proteins by:





36. DNA supercoiling is controlled by:





37. RNA tertiary structures often require:





38. Protein crystallization is essential for:





39. The heme group in hemoglobin is an example of a:





40. Protein secondary structure content is often expressed as:





41. Amyloid fibrils are associated with:





42. The term “macromolecule” in biology usually refers to:





43. The ribosome is best described as a:





44. DNA base stacking contributes to:





45. Protein–DNA binding specificity is largely determined by:





46. Enzyme kinetics are influenced by:





47. Which method measures molecular mass and shape in solution?





48. Chaperonins differ from small chaperones by:





49. Ribozymes are:





50. Cryo-electron microscopy is increasingly used for: