Abstract
Transverse relaxation-optimized NMR experiment (TROSY) for the measurement of three-bond scalar coupling constant between 1Hαi−1 and 15Ni defining the dihedral angle ψ is described. The triple-spin-state-selective experiment allows measurement of 3JHαN from 13Cα, 15N, and 1HN correlation spectra H2O with minimum resonance overlap. Transverse relaxation of 13Cα spin is minimized by using spin-state-selective filtering and by acquiring a signal longer in 15N-dimension in a manner of semi-constant-time TROSY evolution. The 3JHαN values obtained with the proposed α/β-HN(CO)CA-J TROSY scheme are in good agreement with the values measured earlier from ubiquitin in D2O using the HCACO[N] experiment.
| Original language | English |
|---|---|
| Pages (from-to) | 255-259 |
| Journal | Journal of Magnetic Resonance |
| Volume | 146 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 2000 |
| MoE publication type | A1 Journal article-refereed |
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Permi, P., Kilpeläinen, I., & Annila, A. (2000). Determination of backbone angle ψ in proteins using a TROSY-based α/β-HN(CO)CA-J experiment. Journal of Magnetic Resonance, 146(2), 255-259. https://doi.org/10.1006/jmre.2000.2157