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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

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Official URL: http://dx.doi.org/10.1038/NMETH.1300

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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
Subjects: Q Science > QD Chemistry
Divisions: Faculty of Science > Physics
Journal or Publication Title: Nature Methods
Publisher: Nature Publishing Group
ISSN: 1548-7091
Official Date: March 2009
Dates:
DateEvent
March 2009Published
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

Data sourced from Thomson Reuters' Web of Knowledge

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