Nanomole-scale protein solid-state NMR by breaking intrinsic 1HT1 boundaries
Nanomole-scale protein solid-state NMR by breaking intrinsic 1HT1 boundaries
About this item
Full title
Nanomole-scale protein solid-state NMR by breaking intrinsic 1HT1 boundaries
Author / Creator
Publisher
United States
Journal title
Nature methods, 2009-03, Vol.6 (3), p.215-218
Language
English
Formats
Publication information
Publisher
United States
Subjects
More information
Scope and Contents
Contents
We present an approach that accelerates protein solid-state NMR 5-20-fold using paramagnetic doping to condense data-collection time (to approximately 0.2 s per scan), overcoming a long-standing limitation on slow recycling owing to intrinsic (1)H T(1) longitudinal spin relaxation. Using low-power schemes under magic-angle spinning at 40 kHz, we ob...
Alternative Titles
Full title
Nanomole-scale protein solid-state NMR by breaking intrinsic 1HT1 boundaries
Authors, Artists and Contributors
Identifiers
Primary Identifiers
Record Identifier
TN_cdi_proquest_miscellaneous_66971584
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_proquest_miscellaneous_66971584
Other Identifiers
E-ISSN
1548-7105
DOI
10.1038/nmeth.1300
