ArticleJournal of biomolecular NMR2005
A modified strategy for sequence specific assignment of protein NMR spectra based on amino acid type selective experiments.
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 9 papers.
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Who cites it
9 citing papers in PubMed.
- Facilitating NMR Resonance Assignment with Metabolic Tampering.bioRxiv : the preprint server for biology · 2026Article
- Using temperature coefficients to support resonance assignment of intrinsically disordered proteins.Journal of biomolecular NMR · 2025Article
- Novel NMR Assignment Strategy Reveals Structural Heterogeneity in Solution of the nsP3 HVD Domain of Venezuelan Equine Encephalitis Virus.Molecules (Basel, Switzerland) · 2020Article
- Sensitive and simplified: a combinatorial acquisition of five distinct 2D constant-timeJournal of biomolecular NMR · 2020Article
- FJournal of biomolecular NMR · 2017Article
- Amino acid recognition for automatic resonance assignment of intrinsically disordered proteins.Journal of biomolecular NMR · 2016Article
- New amino acid residue type identification experiments valid for protonated and deuterated proteins.Journal of biomolecular NMR · 2012Article
- Amino acid selective unlabeling for sequence specific resonance assignments in proteins.Journal of biomolecular NMR · 2011Article
- Amino-acid type identification in 15N-HSQC spectra by combinatorial selective 15N-labelling.Journal of biomolecular NMR · 2006Article
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Authors and funding
5 authors.
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Abstract
The determination of the three-dimensional structure of a protein or the study of protein-ligand interactions requires the assignment of all relevant nuclei as an initial step. This is nowadays almost exclusively performed using triple-resonance experiments. The conventional strategy utilizes one or more pairs of three dimensional spectra to obtain redundant information and thus reliable assignments. Here, a modified strategy for obtaining sequence specific assignments based on two dimensional amino acid type selective triple-resonance experiments is proposed. These experiments can be recorded with good resolution in a relatively short time. They provide very specific and redundant information, in particular on sequential connectivities, that drastically increases the ease and reliability of the assignment procedure, done either manually or in an automated fashion. The new strategy is demonstrated with the protein domain PB1 from yeast CDC24p.
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