Abstract
A generalized version of the TROSY experiment allows the spin-state selective editing of the four multiplet components of 15 N- 1 H cross peaks of amide groups in proteins into four different subspectra, with no penalty in sensitivity. An improvement by √2 in sensitivity results, if only two of the four multiplet components are selected. Use of the experiment for the measurement of 1 J HN coupling constants is discussed. A water flip-back version of the experiment is demonstrated with a 45 kDa fragment of 15 N/ 2 H labeled Staphylococcus aureus gyrase B.
| Original language | English |
|---|---|
| Pages (from-to) | 364-367 |
| Number of pages | 4 |
| Journal | Journal of Magnetic Resonance |
| Volume | 133 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - Aug 1998 |
| Externally published | Yes |
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