ArticleJournal of biomolecular NMR2005
Efficient and precise measurement of H(alpha)-C(alpha), C(alpha)-C', C(alpha)-C(beta) and H(N)-N residual dipolar couplings from 2D H(N)-N correlation spectra.
Article in Journal of biomolecular NMR, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- A J-modulated protonless NMR experiment characterizes the conformational ensemble of the intrinsically disordered protein WIP.Journal of biomolecular NMR · 2016Article
- Allosteric regulation of E2:E3 interactions promote a processive ubiquitination machine.The EMBO journal · 2013Article
- The structure of the elicitor Cerato-platanin (CP), the first member of the CP fungal protein family, reveals a double ψβ-barrel fold and carbohydrate binding.The Journal of biological chemistry · 2011Article
- Measurement of one and two bond N-C couplings in large proteins by TROSY-based J-modulation experiments.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2009Article
- The novel fold of scytovirin reveals a new twist for antiviral entry inhibitors.Journal of molecular biology · 2007Article
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Authors and funding
4 authors.
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Abstract
A suite of experiments are presented for the measurement of H(alpha)-C(alpha), C(alpha)-C', C(alpha)-C(beta) and H(N)-N couplings from uniformly 15N, 13C labeled proteins. Couplings are obtained from a series of intensity modulated two-dimensional H(N)-N spectra equivalent to the common 1H-15N-HSQC spectra, alleviating many overlap and assignment issues associated with other techniques. To illustrate the efficiency of this method, H(alpha)-C(alpha), C(alpha)-C', and H(N)-N isotropic scalar couplings were determined for ubiquitin from data collected in less than 4.5 h, C(alpha)-C(beta) data collection required 10 h. The resulting couplings were measured with an average error of +/-0.06, +/-0.05, +/-0.04 and +/-0.10 Hz, respectively. This study also shows H(alpha)-C(alpha) and C(alpha)-C(beta) couplings, valuable because they provide orientation of bond vectors outside the peptide plane, can be measured in a uniform and precise way. Superior accuracy and precision to existing 3D measurements for C(alpha)-C' couplings and increased precision compared to IPAP measurements for H(N)-N couplings are demonstrated. Minor modifications allow for acquisition of modulated H(N)-C' 2D spectra, which can yield additional well resolved peaks and significantly increase the number of measured RDCs for proteins with crowded 1H-15N resonances.
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15692737What OpenQuestion holds
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.