ArticleJournal of biomolecular NMR2014
A decadentate Gd(III)-coordinating paramagnetic cosolvent for protein relaxation enhancement measurement.
Article in Journal of biomolecular NMR, 2014. 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, 18 citations in OpenAlex.
- Accurate measurement of longitudinal paramagnetic relaxation enhancement through division after subtraction.Magnetic resonance letters · 2027Article
- Gadolinium-Based NMR Spin Relaxation Measurements of Near-Surface Electrostatic Potentials of Biomolecules.Journal of the American Chemical Society · 2024Article
- A toxin-deformation dependent inhibition mechanism in the T7SS toxin-antitoxin system of Gram-positive bacteria.Nature communications · 2022Article
- Paramagnetic Chemical Probes for Studying Biological Macromolecules.Chemical reviews · 2022Review
- Recent Developments in Data-Assisted Modeling of Flexible Proteins.Frontiers in molecular biosciences · 2021Review
- NMR characterization of solvent accessibility and transient structure in intrinsically disordered proteins.Journal of biomolecular NMR · 2019Article
- NMR-based investigations into target DNA search processes of proteins.Methods (San Diego, Calif.) · 2018Review
- Theory and practice of using solvent paramagnetic relaxation enhancement to characterize protein conformational dynamics.Methods (San Diego, Calif.) · 2018Article
- Characterization of Protein-Protein Interfaces in Large Complexes by Solid-State NMR Solvent Paramagnetic Relaxation Enhancements.Journal of the American Chemical Society · 2017Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
Solvent paramagnetic relaxation enhancement (sPRE) arises from random collisions between paramagnetic cosolvent and protein of interest. The sPRE can be readily measured, affording protein structure information. However, lack of an inert cosolvent probe may yield sPRE values that are not consistent with protein structure. Here we synthesized a new sPRE probe, triethylenetetraamine hexaacetate trimethylamide gadolinium, or Gd(III)-TTHA-TMA. With a total of 10 coordination sites, this paramagnetic cosovlent eliminates an inner-sphere water molecule that can otherwise transfer relaxation to protein through exchange. With the metal ion centered, the new probe is largely spherical with a radius of 4.0 Å, permitting accurate back calculation of sPRE. The effectiveness Gd(III)-TTHA-TMA as a sPRE probe was demonstrated on three well-studied protein systems.
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Registered trials
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