ArticleJournal of biomolecular NMR2007
Assignment of paramagnetic (15)N-HSQC spectra by heteronuclear exchange spectroscopy.
Article in Journal of biomolecular NMR, 2007. 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.
- Pulse EPR-enabled interpretation of scarce pseudocontact shifts induced by lanthanide binding tags.Journal of biomolecular NMR · 2016Article
- Mechanisms of amyloid formation revealed by solution NMR.Progress in nuclear magnetic resonance spectroscopy · 2015Review
- A systematic study of labelling an α-helix in a protein with a lanthanide using IDA-SH or NTA-SH tags.Journal of biomolecular NMR · 2013Article
- Paramagnetic labelling of proteins and oligonucleotides for NMR.Journal of biomolecular NMR · 2010Review
- Prokaryotic ubiquitin-like protein pup is intrinsically disordered.Journal of molecular biology · 2009Article
- Theory, practice, and applications of paramagnetic relaxation enhancement for the characterization of transient low-population states of biological macromolecules and their complexes.Chemical reviews · 2009Review
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Paramagnetic metal ions in proteins provide a rich source of structural information, but the resonance assignments required to extract the information can be challenging. Here we demonstrate that paramagnetically shifted (15)N-HSQC cross-peaks can be assigned using N(Z)-exchange spectroscopy under conditions in which the paramagnetic form of the protein is in dynamic equilibrium with its diamagnetic form. Even slow exchange of specifically bound metal ions may be detected within the long lifetime of (15)N longitudinal magnetization of large proteins at high magnetic fields. Alternatively, the exchange can be accelerated using an excess of metal ions. In the resulting exchange spectra, paramagnetic (15)N resonances become visible for residues that are not directly observed in a conventional (15)N-HSQC spectrum due to paramagnetic (1)H(N) broadening. The experiments are illustrated by the 30 kDa lanthanide-binding epsilon186/theta complex of DNA polymerase III in the presence of sub-stoichiometric amounts of Dy(3+) or a mixture of Dy(3+) and La(3+).
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Registered trials
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