[superscript 15]N-[superscript 15]N Proton Assisted Recoupling in Magic Angle Spinning NMR
Author(s)Lewandowski, Jozef R.; Paepe, Gael De; Eddy, Matthew Thomas; Griffin, Robert Guy
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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).
DepartmentMassachusetts Institute of Technology. Department of Chemistry; Francis Bitter Magnet Laboratory (Massachusetts Institute of Technology)
Journal of the American Chemical Society
American Chemical Society (ACS)
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.
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