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(15)N-(15)N proton assisted recoupling in magic angle spinning NMR.


ABSTRACT: We describe a new magic angle spinning (MAS) NMR experiment for obtaining (15)N-(15)N correlation spectra. The approach yields direct information about the secondary and tertiary structure of proteins, including identification of alpha-helical stretches and interstrand connectivity in antiparallel beta-sheets, which are of major interest for structural studies of membrane proteins and amyloid fibrils. The method, (15)N-(15)N proton assisted recoupling (PAR), relies on a second-order mechanism, third spin assisted recoupling (TSAR), used previously in the context of (15)N-(13)C and (13)C-(13)C polarization transfer schemes. In comparison to (15)N-(15)N proton-driven spin diffusion experiments, the PAR technique accelerates polarization transfer between (15)N's by a factor of approximately 10(2)-10(3) and is furthermore applicable over the entire range of currently available MAS frequencies (10-70 kHz).

SUBMITTER: Lewandowski JR 

PROVIDER: S-EPMC2754755 | biostudies-literature | 2009 Apr

REPOSITORIES: biostudies-literature

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(15)N-(15)N proton assisted recoupling in magic angle spinning NMR.

Lewandowski Józef R JR   De Paëpe Gaël G   Eddy Matthew T MT   Griffin Robert G RG  

Journal of the American Chemical Society 20090401 16


We describe a new magic angle spinning (MAS) NMR experiment for obtaining (15)N-(15)N correlation spectra. The approach yields direct information about the secondary and tertiary structure of proteins, including identification of alpha-helical stretches and interstrand connectivity in antiparallel beta-sheets, which are of major interest for structural studies of membrane proteins and amyloid fibrils. The method, (15)N-(15)N proton assisted recoupling (PAR), relies on a second-order mechanism, t  ...[more]

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