[superscript 15]N-[superscript 15]N Proton Assisted Recoupling in Magic Angle Spinning NMR
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Griffin_N15-N15 proton.pdf
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Author(s)
Lewandowski, Jozef R.
Paepe, Gael De
Eddy, Matthew Thomas
Griffin, Robert Guy
Date Issued
April 2009
Journal
Journal of the American Chemical Society
Publisher
American Chemical Society (ACS)
Citation
Lewandowski, Jozef R., Gael De Paepe, Matthew T. Eddy, and Robert G. Griffin. “15N−15N Proton Assisted Recoupling in Magic Angle Spinning NMR.” Journal of the American Chemical Society 131, no. 16 (April 29, 2009): 5769-5776.
Version
Author's final manuscript
Abstract
We describe a new magic angle spinning (MAS) NMR experiment for obtaining [superscript 15]N−[superscript 15]N correlation spectra. The approach yields direct information about the secondary and tertiary structure of proteins, including identification of α-helical stretches and interstrand connectivity in antiparallel β-sheets, which are of major interest for structural studies of membrane proteins and amyloid fibrils. The method, [superscript 15]N−[superscript 15]N proton assisted recoupling (PAR), relies on a second-order mechanism, third spin assisted recoupling (TSAR), used previously in the context of [superscript 15]N−[superscript 13]C and [superscript 13]C−[superscript 13]C polarization transfer schemes. In comparison to [superscript 15]N−[superscript 15]N proton-driven spin diffusion experiments, the PAR technique accelerates polarization transfer between [superscript 15]N’s by a factor of ~10[superscript 2]−10[superscript 3] and is furthermore applicable over the entire range of currently available MAS frequencies (10−70 kHz).
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
Francis Bitter Magnet Laboratory (Massachusetts Institute of Technology)
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DOI of Published Version
https://doi.org/10.1021/ja806578y
