Nanomole-scale protein solid-state NMR by breaking intrinsic 1HT1 boundaries.
We present an approach that accelerates protein solid-state NMR 5-20-fold using paramagnetic doping to condense data-collection time (to approximately 0.2 s per scan), overcoming a long-standing limitation on slow recycling owing to intrinsic (1)H T(1) longitudinal spin relaxation. Using low-power schemes under magic-angle spinning at 40 kHz, we obtained two-dimensional (13)C-(13)C and (13)C-(15)N solid-state NMR spectra for several to tens of nanomoles of beta-amyloid fibrils and ubiquitin in 1-2 d.
Wickramasinghe
Nalinda P
NP
Department of Chemistry, University of Illinois at Chicago, 845 West Taylor Street, Chicago, IL 60607, USA.
Parthasarathy
Sudhakar
S
Jones
Christopher R
CR
Bhardwaj
Chhavi
C
Long
Fei
F
Kotecha
Mrignayani
M
Mehboob
Shahila
S
Fung
Leslie W-M
LW
Past
Jaan
J
Samoson
Ago
A
Ishii
Yoshitaka
Y
D000682:Amyloid / Q000737:chemistry; D016229:Amyloid beta-Peptides / Q000737:chemistry; D002247:Carbon Isotopes / Q000737:chemistry; D004492:Edetic Acid / Q000737:chemistry; D006801:Humans; D009587:Nitrogen Isotopes / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010446:Peptide Fragments / Q000737:chemistry; D011487:Protein Conformation; D013049:Spectrin / Q000737:chemistry; D025801:Ubiquitin / Q000737:chemistry
D000682:Amyloid; D016229:Amyloid beta-Peptides; D002247:Carbon Isotopes; D009587:Nitrogen Isotopes; D010446:Peptide Fragments; D025801:Ubiquitin; C078592:amyloid beta-protein (1-40); C075222:amyloid beta-protein (1-42); D013049:Spectrin; D004492:Edetic Acid