Assignment of methyl NMR resonances of a 52 kDa protein with residue-specific 4D correlation maps
| Autor: | Subrata H. Mishra, Dominique P. Frueh |
|---|---|
| Rok vydání: | 2015 |
| Předmět: |
chemistry.chemical_classification
Chemistry Stereochemistry Proteins Resonance Covariance Biochemistry Article Spectral line Amino acid chemistry.chemical_compound Nuclear magnetic resonance Nonribosomal peptide Valine Amide Isoleucine Nuclear Magnetic Resonance Biomolecular Amino Acids Branched-Chain Spectroscopy |
| Zdroj: | Journal of Biomolecular NMR. 62:281-290 |
| ISSN: | 1573-5001 0925-2738 |
| DOI: | 10.1007/s10858-015-9943-6 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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