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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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
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author 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
author_facet 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
author_sort Wickramasinghe, Nalinda P.
collection PubMed
description 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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spelling pubmed-26497012009-09-01 Nanomole-scale Protein Solid-state NMR by Breaking Intrinsic (1)H-T(1) Boundaries 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 Nat Methods Article 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. 2009-02-08 2009-03 /pmc/articles/PMC2649701/ /pubmed/19198596 http://dx.doi.org/10.1038/nmeth.1300 Text en http://www.nature.com/authors/editorial_policies/license.html#terms Users may view, print, copy, and download text and data-mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use:http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
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
Nanomole-scale Protein Solid-state NMR by Breaking Intrinsic (1)H-T(1) Boundaries
title Nanomole-scale Protein Solid-state NMR by Breaking Intrinsic (1)H-T(1) Boundaries
title_full Nanomole-scale Protein Solid-state NMR by Breaking Intrinsic (1)H-T(1) Boundaries
title_fullStr Nanomole-scale Protein Solid-state NMR by Breaking Intrinsic (1)H-T(1) Boundaries
title_full_unstemmed Nanomole-scale Protein Solid-state NMR by Breaking Intrinsic (1)H-T(1) Boundaries
title_short Nanomole-scale Protein Solid-state NMR by Breaking Intrinsic (1)H-T(1) Boundaries
title_sort nanomole-scale protein solid-state nmr by breaking intrinsic (1)h-t(1) boundaries
topic Article
url 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
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