ArticleJournal of biomolecular NMR2010
HNCO-based measurement of one-bond amide 15N-1H couplings with optimized precision.
Article in Journal of biomolecular NMR, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- 2D (1)H(N), (15)N Correlated NMR Methods at Natural Abundance for Obtaining Structural Maps and Statistical Comparability of Monoclonal Antibodies.Pharmaceutical research · 2016Article
- NMR methods for structural studies of large monomeric and multimeric proteins.Current opinion in structural biology · 2013Review
- RDC derived protein backbone resonance assignment using fragment assembly.Journal of biomolecular NMR · 2011Article
- Facile measurement of ¹H-¹5N residual dipolar couplings in larger perdeuterated proteins.Journal of biomolecular NMR · 2010Article
- Cooperative formation of native-like tertiary contacts in the ensemble of unfolded states of a four-helix protein.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- MQ-HNCO-TROSY for the measurement of scalar and residual dipolar couplings in larger proteins: application to a 557-residue IgFLNa16-21.Journal of biomolecular NMR · 2010Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
A pair of 3D HNCO-based experiments have been developed with the aim of optimizing the precision of measurement of (1)J(NH) couplings. Both pulse sequences record (1)J(NH) coupling evolution during the entire constant time interval that (15)N magnetization is dephasing or rephasing with respect to the directly bonded (13)C' nucleus, with (15)N(13)C' multiple quantum coherence maintained during the (13)C' evolution period. The first experiment, designed for smaller proteins, produces an apparent doubling of the (1)J(NH) coupling without any accompanying increases in line width. The second experiment is a J-scaled TROSY-HNCO experiment in which the (1)J(NH) coupling is measured by frequency difference between resonances offset symmetrically about the position of the downfield component of the (15)N doublet (i.e. the TROSY resonance). This experiment delivers significant gains in precision of (1)J(NH) coupling measurement compared to existing J-scaled TROSY-HNCO experiments. With the proper choice of acquisition parameters and sufficient sensitivity to acquire a 3D TROSY-HNCO experiment, it is shown that (1)J(NH) couplings can be measured with a precision which approaches or exceeds the precision of measurement with which the frequency of the TROSY resonance itself can be determined.
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