Determination of Backbone Angle ψ in Proteins Using a TROSY-Based α/β-HN(CO)CA-J Experiment
✍ Scribed by Perttu Permi; Ilkka Kilpeläinen; Arto Annila
- Publisher
- Elsevier Science
- Year
- 2000
- Tongue
- English
- Weight
- 117 KB
- Volume
- 146
- Category
- Article
- ISSN
- 1090-7807
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✦ Synopsis
Transverse relaxation-optimized NMR experiment (TROSY) for the measurement of three-bond scalar coupling constant between 1 H i؊1 ␣ and 15 N i defining the dihedral angle is described. The triple-spin-state-selective experiment allows measurement of 3 J H ␣ N from 13 C ␣ , 15 N, and 1 H N correlation spectra H 2 O with minimum resonance overlap. Transverse relaxation of 13 C ␣ spin is minimized by using spin-state-selective filtering and by acquiring a signal longer in 15 N-dimension in a manner of semi-constant-time TROSY evolution. The 3 J H ␣ N values obtained with the proposed ␣/-HN(CO)CA-J TROSY scheme are in good agreement with the values measured earlier from ubiquitin in D 2 O using the HCACO[N] experiment.