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Three-Dimensional 13C Shift/1H–15N Coupling/15N Shift Solid-State NMR Correlation Spectroscopy

✍ Scribed by Zhengtian Gu; Stanley J. Opella

Publisher
Elsevier Science
Year
1999
Tongue
English
Weight
83 KB
Volume
138
Category
Article
ISSN
1090-7807

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✦ Synopsis

Triple-resonance experiments capable of correlating directly bonded and proximate carbon and nitrogen backbone sites of uniformly 13 C-and 15 N-labeled peptides in stationary oriented samples are described. The pulse sequences integrate cross-polarization from 1 H to 13 C and from 13 C to 15 N with flip-flop (phase and frequency switched) Lee-Goldburg irradiation for both 13 C homonuclear decoupling and 1 H-15 N spin exchange at the magic angle. Because heteronuclear decoupling is applied throughout, the three-dimensional pulse sequence yields 13 C shift/ 1 H-15 N coupling/ 15 N shift correlation spectra with single-line resonances in all three frequency dimensions. Not only do the three-dimensional spectra correlate 13 C and 15 N resonances, they are well resolved due to the three independent frequency dimensions, and they can provide up to four orientationally dependent frequencies as input for structure determination. These experiments have the potential to make sequential backbone resonance assignments in uniformly 13 C-and 15 N-labeled proteins.

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