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

Full text not available from this repository, contact author.

Request Changes to record.

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:	Date Event March 2009 Published
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

Request changes or add full text files to a record

Repository staff actions (login required)

View Item