Nanomole-scale Protein Solid-state NMR by Breaking Intrinsic (1)H-T(1) Boundaries

We present an approach that speeds up protein solid-state NMR (SSNMR) by 5–20 fold by using paramagnetic doping to condense data-collection time (to ~0.2 s/scan), overcoming a long-standing limitation on slow recycling due to intrinsic (1)H T(1) longitudinal spin relaxation. By employing low-power s...

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Detalles Bibliográficos
Autores principales: Wickramasinghe, Nalinda P., Parthasarathy, Sudhakar, Jones, Christopher R., Bhardwaj, Chhavi, Long, Fei, Kotecha, Mrignayani, Mehboob, Shahila, Fung, Leslie W.-M, Past, Jaan, Samoson, Ago, Ishii, Yoshitaka
Formato: Texto
Lenguaje:English
Publicado: 2009
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2649701/
https://www.ncbi.nlm.nih.gov/pubmed/19198596
http://dx.doi.org/10.1038/nmeth.1300
Descripción
Sumario:We present an approach that speeds up protein solid-state NMR (SSNMR) by 5–20 fold by using paramagnetic doping to condense data-collection time (to ~0.2 s/scan), overcoming a long-standing limitation on slow recycling due to intrinsic (1)H T(1) longitudinal spin relaxation. By employing low-power schemes under magic-angle spinning at 40 kHz, we show that two-dimensional (13)C/(13)C and (13)C/(15)N SSNMR spectra can be attained for several to tens of nano-moles of β-amyloid fibrils and ubiquitin in just 1–2 days.

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