Research Article
J-based 2D homonuclear and heteronuclear correlation in solid-state proteins
Article first published online: 21 DEC 2007
DOI: 10.1002/mrc.2107
Copyright © 2007 John Wiley & Sons, Ltd.
Issue
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Magnetic Resonance in Chemistry
Special Issue: New techniques in solid-state NMR
Volume 45, Issue S1, pages S84–S92, December 2007
Additional Information
How to Cite
Chen, L., Kaiser, J. M., Lai, J., Polenova, T., Yang, J., Rienstra, C. M. and Mueller, L. J. (2007), J-based 2D homonuclear and heteronuclear correlation in solid-state proteins. Magn. Reson. Chem., 45: S84–S92. doi: 10.1002/mrc.2107
Publication History
- Issue published online: 21 DEC 2007
- Article first published online: 21 DEC 2007
- Manuscript Accepted: 17 SEP 2007
- Manuscript Revised: 9 SEP 2007
- Manuscript Received: 30 JUL 2007
- Abstract
- References
- Cited By
Keywords:
- NMR;
- 13C;
- 15N;
- solid-state NMR;
- scalar-coupling-driven correlation;
- through-bond correlation;
- protein
Abstract
Scalar-based two-dimensional heteronuclear experiments are reported for NCO and NCA chemical shift correlation in the solid state. In conjunction with homonuclear CACO correlation, these experiments form a useful set for tracing connectivities and assigning backbone resonances in solid-state proteins. The applicability of this approach is demonstrated on two proteins, the β 1 immunoglobulin binding domain of protein G at 9.4 T and reassembled thioredoxin at 14.1 T, using different decoupling conditions and MAS frequencies. These constant-time J-based correlation experiments exhibit increased resolution in the indirect dimension owing to homonuclear and heteronuclear decoupling, and because the indirect evolution and transfer periods are combined into a single constant time interval, this increased resolution is not obtained at the cost of sensitivity. These experiments are also shown to be compatible with in-phase anti-phase (IPAP) selection, giving increased resolution in the directly detected dimension. Copyright © 2007 John Wiley & Sons, Ltd.

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