ArticleJournal of the American Chemical Society2007
Bound-state residual dipolar couplings for rapidly exchanging ligands of His-tagged proteins.
Article in Journal of the American Chemical Society, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed, 22 citations in OpenAlex.
- Application of Relaxation Dispersion of HyperpolarizedAngewandte Chemie (International ed. in English) · 2021Article
- Protein structure validation and identification from unassigned residual dipolar coupling data using 2D-PDPA.Molecules (Basel, Switzerland) · 2013Article
- The use of residual dipolar coupling in studying proteins by NMR.Topics in current chemistry · 2012Review
- Nuclear magnetic resonance structural characterization of substrates bound to the alpha-2,6-sialyltransferase, ST6Gal-I.Biochemistry · 2009Article
- Structure determination of a Galectin-3-carbohydrate complex using paramagnetism-based NMR constraints.Protein science : a publication of the Protein Society · 2008Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The study of bound-state conformations of ligands interacting with proteins is important to the understanding of protein function and the design of drugs that alter function. Traditionally, transferred nuclear Overhauser effects (trNOEs), measured from NMR spectra of ligands in rapid exchange between bound and free states, have been used in these studies, owing to the inherent heavy weighting of bound-state data in the averaged ligand signals. In principle, residual dipolar couplings (RDCs) provide a useful complement to NOE data in that they provide orientational constraints as opposed to distance constraints, but use in ligand-binding applications has been limited due to the absence of heavy weighting of bound-state data. A widely applicable approach to increasing the weighting of bound-state data in averaged RDCs measured on ligands is presented. The approach rests on association of a His-tagged protein with a nickel-chelate-carrying lipid inserted into the lipid bilayer-like alignment media used in the acquisition of RDCs. The approach is validated through the observation of bound-state RDCs for the disaccharide, lactose, bound to the carbohydrate recognition domain of the mammalian lectin, galectin-3.
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Registered trials
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