ArticleJournal of biomolecular NMR2015
Assignment of methyl NMR resonances of a 52 kDa protein with residue-specific 4D correlation maps.
Article in Journal of biomolecular NMR, 2015. 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.
- Global protein dynamics as communication sensors in peptide synthetase domains.Science advances · 2022Article
- Minimizing Pervasive Artifacts in 4D Covariance Maps for Protein Side Chain NMR Assignments.The journal of physical chemistry. A · 2021Article
- Emerging solution NMR methods to illuminate the structural and dynamic properties of proteins.Current opinion in structural biology · 2019Review
- NMR assignments of sparsely labeled proteins using a genetic algorithm.Journal of biomolecular NMR · 2017Article
- Covariance nuclear magnetic resonance methods for obtaining protein assignments and novel correlations.Concepts in magnetic resonance. Part A, Bridging education and research · 2017Article
- Effortless assignment with 4D covariance sequential correlation maps.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015Article
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Authors and funding
2 authors.
Funding
Abstract
Methyl groups have become key probes for structural and functional studies by nuclear magnetic resonance. However, their NMR signals cluster in a small spectral region and assigning their resonances can be a tedious process. Here, we present a method that facilitates assignment of methyl resonances from assigned amide groups. Calculating the covariance between sensitive methyl and amide 3D spectra, each providing correlations to C(α) and C(β) separately, produces 4D correlation maps directly correlating methyl groups to amide groups. Optimal correlation maps are obtained by extracting residue-specific regions, applying derivative to the dimensions subject to covariance, and multiplying 4D maps stemming from different 3D spectra. The latter procedure rescues weak signals that may be missed in traditional assignment procedures. Using these covariance correlation maps, nearly all assigned isoleucine, leucine, and valine amide resonances of a 52 kDa nonribosomal peptide synthetase cyclization domain were paired with their corresponding methyl groups.
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