Determination of backbone angle ψ in proteins using a TROSY-based α/β-HN(CO)CA-J experiment

Perttu Permi (Corresponding Author), Ilkka Kilpeläinen, Arto Annila

Research output: Contribution to journalArticleScientificpeer-review

16 Citations (Scopus)


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 languageEnglish
Pages (from-to)255-259
JournalJournal of Magnetic Resonance
Issue number2
Publication statusPublished - 2000
MoE publication typeA1 Journal article-refereed


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