Transverse relaxation optimised spin-state selective NMR experiments for measurement of residual dipolar couplings

P. Permi, Arto Annila

Research output: Contribution to journalArticleScientificpeer-review

52 Citations (Scopus)

Abstract

Three transverse relaxation optimised NMR experiments (TROSY) for the measurement of scalar and dipolar couplings suitable for proteins dissolved in aqueous iso- and anisotropic solutions are described. The triple-spin-state-selective experiments yield couplings between 1HN-13Cα, 15N-13Cα, 1HN-13Cαi−1, 15N-13Cαi−1, 1HN-13C′i−1, 15N-13C′i−1, and 13C′i−1-13Cαi−1 without introducing nonessential spectral crowding compared with an ordinary two-dimensional 15N-1H correlation spectrum and without requiring explicit knowledge of carbon assignments. This set of α/β-J-TROSY experiments is most useful for perdeuterated proteins in studies of structure–activity relationships by NMR to observe, in addition to epitopes for ligands, also conformational changes induced by binding of ligands.

Original languageEnglish
Pages (from-to)221 - 227
Number of pages7
JournalJournal of Biomolecular NMR
Volume16
Issue number3
DOIs
Publication statusPublished - 2000
MoE publication typeA1 Journal article-refereed

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Nuclear magnetic resonance
Ligands
Epitopes
Proteins
Carbon
Experiments

Cite this

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abstract = "Three transverse relaxation optimised NMR experiments (TROSY) for the measurement of scalar and dipolar couplings suitable for proteins dissolved in aqueous iso- and anisotropic solutions are described. The triple-spin-state-selective experiments yield couplings between 1HN-13Cα, 15N-13Cα, 1HN-13Cαi−1, 15N-13Cαi−1, 1HN-13C′i−1, 15N-13C′i−1, and 13C′i−1-13Cαi−1 without introducing nonessential spectral crowding compared with an ordinary two-dimensional 15N-1H correlation spectrum and without requiring explicit knowledge of carbon assignments. This set of α/β-J-TROSY experiments is most useful for perdeuterated proteins in studies of structure–activity relationships by NMR to observe, in addition to epitopes for ligands, also conformational changes induced by binding of ligands.",
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Transverse relaxation optimised spin-state selective NMR experiments for measurement of residual dipolar couplings. / Permi, P.; Annila, Arto.

In: Journal of Biomolecular NMR, Vol. 16, No. 3, 2000, p. 221 - 227.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Transverse relaxation optimised spin-state selective NMR experiments for measurement of residual dipolar couplings

AU - Permi, P.

AU - Annila, Arto

PY - 2000

Y1 - 2000

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AB - Three transverse relaxation optimised NMR experiments (TROSY) for the measurement of scalar and dipolar couplings suitable for proteins dissolved in aqueous iso- and anisotropic solutions are described. The triple-spin-state-selective experiments yield couplings between 1HN-13Cα, 15N-13Cα, 1HN-13Cαi−1, 15N-13Cαi−1, 1HN-13C′i−1, 15N-13C′i−1, and 13C′i−1-13Cαi−1 without introducing nonessential spectral crowding compared with an ordinary two-dimensional 15N-1H correlation spectrum and without requiring explicit knowledge of carbon assignments. This set of α/β-J-TROSY experiments is most useful for perdeuterated proteins in studies of structure–activity relationships by NMR to observe, in addition to epitopes for ligands, also conformational changes induced by binding of ligands.

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DO - 10.1023/A:1008362211560

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