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.
Original language | English (US) |
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Pages (from-to) | S84-S92 |
Journal | Magnetic Resonance in Chemistry |
Volume | 45 |
Issue number | SUPPL. |
DOIs | |
State | Published - Dec 2007 |
Keywords
- C
- N
- NMR
- Protein
- Scalar-coupling-driven correlation
- Solid-state NMR
- Through-bond correlation
ASJC Scopus subject areas
- Chemistry(all)
- Materials Science(all)