ArticleJournal of biomolecular NMR2007
Measurement of dissociation constants of high-molecular weight protein-protein complexes by transferred 15N-relaxation.
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 12 papers.
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Who cites it
12 citing papers in PubMed.
- Atomistic modulation of MIF-2 structure, catalysis, and biological signaling via cysteine residues and a small molecule, Ebselen.Protein science : a publication of the Protein Society · 2025Article
- The Complementarity of Nuclear Magnetic Resonance and Native Mass Spectrometry in Probing Protein-Protein Interactions.Advances in experimental medicine and biology · 2024Review
- SARS-CoV-2 Nsp8 N-terminal domain folds autonomously and binds dsRNA.Nucleic acids research · 2023Article
- Segmental structural dynamics in Aβ42 globulomers.Biochemical and biophysical research communications · 2021Article
- Leiomodin creates a leaky cap at the pointed end of actin-thin filaments.PLoS biology · 2020Article
- Article
- Engineering [Ln(DPA)3] 3- binding sites in proteins: a widely applicable method for tagging proteins with lanthanide ions.Journal of biomolecular NMR · 2011Article
- Elucidating slow binding kinetics of a protein without observable bound resonances by longitudinal relaxation NMR spectroscopy.Journal of biomolecular NMR · 2011Article
- Using NMR to distinguish viscosity effects from nonspecific protein binding under crowded conditions.Journal of the American Chemical Society · 2009Article
- The unstructured C-terminus of the tau subunit of Escherichia coli DNA polymerase III holoenzyme is the site of interaction with the alpha subunit.Nucleic acids research · 2007Article
- Solution structure of Domains IVa and V of the tau subunit of Escherichia coli DNA polymerase III and interaction with the alpha subunit.Nucleic acids research · 2007Article
- Polyubiquitin and ubiquitin-like signals share common recognition sites on proteasomal subunit Rpn1.The Journal of biological chemistryArticle
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Authors and funding
6 authors.
Funding
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Abstract
The use of (15)N-relaxation data for determination of the dissociation constant of a protein-protein complex is proposed for the situation where a (15)N-labeled protein is bound to an unlabeled protein of high molecular weight, and the chemical exchange between bound and free protein is fast on the NMR time scale. The approach is shown to be suitable for estimating dissociation constants in the micromolar to millimolar range, using protein solutions at relatively low concentration. An example is shown for the interaction between two subunits from the Escherichia coli DNA polymerase III complex, involving a (15)N-labeled fragment of the C-terminal domain of the tau subunit (15 kDa) and the unlabeled alpha subunit (130 kDa).
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.