ArticleJournal of magnetic resonance (San Diego, Calif. : 1997)2010
Measurement and interpretation of 15N-1H residual dipolar couplings in larger proteins.
Article in Journal of magnetic resonance (San Diego, Calif. : 1997), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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Who cites it
5 citing papers in PubMed.
- Solution NMR Experiment for Measurement of (15)N-(1)H Residual Dipolar Couplings in Large Proteins and Supramolecular Complexes.Journal of the American Chemical Society · 2015Article
- NMR methods for structural studies of large monomeric and multimeric proteins.Current opinion in structural biology · 2013Review
- Measurement of (1)H-(15)N and (1)H-(13)C residual dipolar couplings in nucleic acids from TROSY intensities.Journal of biomolecular NMR · 2011Article
- 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
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
A decade ago, Dr. L.E. Kay and co-workers described an ingenious HNCO-based triple-resonance experiment from which several protein backbone RDCs can be measured simultaneously (Yang et al. (1999) [1]). They implemented a J-scaling technique in the (15)N dimension of the 3D experiment to obtain the NH RDCs. We have used this idea to carry out J-scaling in a 2D (15)N-(1)H-TROSY experiment and have found it to be an excellent method to obtain NH RDCs for larger proteins upto 70 kDa, far superior to commonly used HSQC in-phase/anti-phase and HSQC/TROSY comparisons. Here, this method, dubbed "RDC-TROSY" is discussed in detail and the limits of its utility are assessed by simulations. Prominent in the latter analysis is the evaluation of the effect of amide proton flips on the "RDC-TROSY" linewidths. The details of the technical and computational implementations of these methods for the determination of domain orientations in 45-60 kDa Hsp70 chaperone protein constructs are described.
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Registered trials
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