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Nanomole-scale protein solid-state NMR by breaking intrinsic 1HT1 boundaries.

ABSTRACT: 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.

SUBMITTER: Wickramasinghe NP

PROVIDER: S-EPMC2649701 | biostudies-literature | 2009 Mar

REPOSITORIES: biostudies-literature

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Nanomole-scale protein solid-state NMR by breaking intrinsic 1HT1 boundaries.

Wickramasinghe Nalinda P NP 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

Nature methods 20090208 3

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 ...[more]

PMID: 19198596

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