Discussion
Why do large molecules such as proteins give broad NMR lines?
Answer: A
Slow molecular tumbling makes the dipolar interaction average less completely, so transverse relaxation is efficient, T2 is short and lines are broad. The effect grows with molecular mass and is the principal barrier to NMR of very large assemblies, addressed by deuteration, high field and specialised experiments. Quadrupolar nuclei are no more common in proteins, shift dispersion is if anything an advantage in a folded protein, and concentration affects viscosity only indirectly. Correlation time is the governing quantity throughout.
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