Nanomole-scale protein solid-state NMR by breaking intrinsic 1H T1 boundaries.

We present an approach that accelerates protein solid-state NMR 5–20-fold using paramagnetic doping to condense data-collection time (to ∼0.2 s per scan), overcoming a long-standing limitation on slow recycling owing to intrinsic ¹H T₁ longitudinal spin relaxation. Using low-power schemes under magic-angle spinning at 40 kHz, we obtained two-dimensional ¹³C-¹³C and ¹³C-¹⁵N solid-state NMR spectra for several to tens of nanomoles of β-amyloid fibrils and ubiquitin in 1–2 d. [ABSTRACT FROM AUTHOR]