ArticleJournal of magnetic resonance (San Diego, Calif. : 1997)2010
A practical implementation of cross-spectrum in protein backbone resonance assignment.
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 6 papers.
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Who cites it
6 citing papers in PubMed.
- Minimizing Pervasive Artifacts in 4D Covariance Maps for Protein Side Chain NMR Assignments.The journal of physical chemistry. A · 2021Article
- Covariance nuclear magnetic resonance methods for obtaining protein assignments and novel correlations.Concepts in magnetic resonance. Part A, Bridging education and research · 2017Article
- Assignment of methyl NMR resonances of a 52 kDa protein with residue-specific 4D correlation maps.Journal of biomolecular NMR · 2015Article
- Exploiting image registration for automated resonance assignment in NMR.Journal of biomolecular NMR · 2015Article
- Facilitated assignment of large protein NMR signals with covariance sequential spectra using spectral derivatives.Journal of the American Chemical Society · 2014Article
- Deconvolution of chemical mixtures with high complexity by NMR consensus trace clustering.Analytical chemistry · 2011Article
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3 authors.
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Abstract
The concept of cross-spectrum is applied in protein NMR spectroscopy to assist in the backbone sequential resonance assignment. Cross-spectrum analysis is used routinely to reveal correlations in frequency domains as a means to reveal common features contained in multiple time series. Here the cross-spectrum between related NMR spectra, for example HNCO and HN(CA)CO, can be calculated with point-by-point multiplications along their common C' carbon axis. In the resulting higher order cross-spectrum, an enhanced correlation signal occurs at every common i-1 carbon frequency allowing the amide proton H(N) (and nitrogen N) resonances from residues i and i-1 to be identified. The cross-spectrum approach is demonstrated using 2D spectra H(N)CO, H(NCA)CO, H(NCO)CACB, and H(N)CACB measured on a 15N/13C double-labeled Ubiquitin sample. These 2D spectra are used to calculate two pseudo-3D cross-spectra, H(i)-H(i)(-1)-C'(i)(-1) and H(i)-H(i)(-1)-CA(i)(-1)CB(i)(-1). We show using this approach, backbone resonances of H, C', CA, and CB can be fully assigned without ambiguity. The cross-spectrum principle is expected to offer an easy, practical, and more quantitative approach for heteronuclear backbone resonance assignment.
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