ArticleJournal of biomolecular NMR2007
HIFI-C: a robust and fast method for determining NMR couplings from adaptive 3D to 2D projections.
Article in Journal of biomolecular NMR, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Sensitivity enhancement in solution NMR: emerging ideas and new frontiers.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014Review
- Nonuniform sampling and maximum entropy reconstruction in multidimensional NMR.Accounts of chemical research · 2014Article
- Radial sampling for fast NMR: Concepts and practices over three decades.Progress in nuclear magnetic resonance spectroscopy · 2010Review
- NMR in a crystallography-based high-throughput protein structure-determination environment.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010Article
- Biomolecular NMR data analysis.Progress in nuclear magnetic resonance spectroscopy · 2010Review
- Highly automated protein backbone resonance assignment within a few hours: the "BATCH" strategy and software package.Journal of biomolecular NMR · 2009Article
- The Center for Eukaryotic Structural Genomics.Journal of structural and functional genomics · 2009Article
- APSY-NMR with proteins: practical aspects and backbone assignment.Journal of biomolecular NMR · 2008Article
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5 authors.
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Abstract
We describe a novel method for the robust, rapid, and reliable determination of J couplings in multi-dimensional NMR coupling data, including small couplings from larger proteins. The method, "High-resolution Iterative Frequency Identification of Couplings" (HIFI-C) is an extension of the adaptive and intelligent data collection approach introduced earlier in HIFI-NMR. HIFI-C collects one or more optimally tilted two-dimensional (2D) planes of a 3D experiment, identifies peaks, and determines couplings with high resolution and precision. The HIFI-C approach, demonstrated here for the 3D quantitative J method, offers vital features that advance the goal of rapid and robust collection of NMR coupling data. (1) Tilted plane residual dipolar couplings (RDC) data are collected adaptively in order to offer an intelligent trade off between data collection time and accuracy. (2) Data from independent planes can provide a statistical measure of reliability for each measured coupling. (3) Fast data collection enables measurements in cases where sample stability is a limiting factor (for example in the presence of an orienting medium required for residual dipolar coupling measurements). (4) For samples that are stable, or in experiments involving relatively stronger couplings, robust data collection enables more reliable determinations of couplings in shorter time, particularly for larger biomolecules. As a proof of principle, we have applied the HIFI-C approach to the 3D quantitative J experiment to determine N-C' RDC values for three proteins ranging from 56 to 159 residues (including a homodimer with 111 residues in each subunit). A number of factors influence the robustness and speed of data collection. These factors include the size of the protein, the experimental set up, and the coupling being measured, among others. To exhibit a lower bound on robustness and the potential for time saving, the measurement of dipolar couplings for the N-C' vector represents a realistic "worst case analysis". These couplings are among the smallest currently measured, and their determination in both isotropic and anisotropic media demands the highest measurement precision. The new approach yielded excellent quantitative agreement with values determined independently by the conventional 3D quantitative J NMR method (in cases where sample stability in oriented media permitted these measurements) but with a factor of 2-5 in time savings. The statistical measure of reliability, measuring the quality of each RDC value, offers valuable adjunct information even in cases where modest time savings may be realized.
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