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Nanomole-scale protein solid-state NMR by breaking intrinsic H-1 T-1 boundaries
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Wickramasinghe, Nalinda P., Parthasarathy, Sudhakar, Jones, Christopher R., Bhardwaj, Chhavi, Long, Fei, Kotecha, Mrignayani, Mehboob, Shahila, Fung, Leslie W-M, Past, Jaan, Samoson, Ago and Ishii, Yoshitaka (2009) Nanomole-scale protein solid-state NMR by breaking intrinsic H-1 T-1 boundaries. Nature Methods, Vol.6 (No.3). pp. 215-218. doi:10.1038/nmeth.1300 ISSN 1548-7091.
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Official URL: http://dx.doi.org/10.1038/NMETH.1300
Abstract
We present an approach that accelerates protein solid-state NMR 5-20-fold using paramagnetic doping to condense datacollection time (to similar to 0.2 s per scan), overcoming a long-standing limitation on slow recycling owing to intrinsic H-1 T-1 longitudinal spin relaxation. Using low-power schemes under magic-angle spinning at 40 kHz, we obtained two-dimensional C-13-C-13 and C-13-N-15 solid-state NMR spectra for several to tens of nanomoles of beta-amyloid fibrils and ubiquitin in 1-2 d.
Item Type: | Journal Article | ||||
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Subjects: | Q Science > QD Chemistry | ||||
Divisions: | Faculty of Science, Engineering and Medicine > Science > Physics | ||||
Journal or Publication Title: | Nature Methods | ||||
Publisher: | Nature Publishing Group | ||||
ISSN: | 1548-7091 | ||||
Official Date: | March 2009 | ||||
Dates: |
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Volume: | Vol.6 | ||||
Number: | No.3 | ||||
Number of Pages: | 4 | ||||
Page Range: | pp. 215-218 | ||||
DOI: | 10.1038/nmeth.1300 | ||||
Status: | Peer Reviewed | ||||
Publication Status: | Published | ||||
Access rights to Published version: | Restricted or Subscription Access | ||||
Funder: | Dreyfus Foundation Teacher-Scholar Award program, US National Science Foundation (CAREER), Alzheimer's Association (IIRG), National Institutes of Health R01 program, Estonian Science foundation programs | ||||
Grant number: | CHE 449952, 08-91256, AG028490 |
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