ArticleJournal of the American Chemical Society2014
Protein apparent dielectric constant and its temperature dependence from remote chemical shift effects.
Article in Journal of the American Chemical Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
5 citing papers in PubMed.
- Chemical exchange saturation transfer NMR: An analytical tool and its applications.Magnetic resonance letters · 2026Review
- Molecular Dynamics Force Field Parameters for the EGFP Chromophore and Some of Its Analogues.The journal of physical chemistry. B · 2023Article
- The Effect of Residual Triton X-100 on Structural Stability and Infection Activity of Adenovirus Particles.Molecular therapy. Methods & clinical development · 2020Article
- Converging nuclear magnetic shielding calculations with respect to basis and system size in protein systems.Journal of biomolecular NMR · 2015Article
- pH-dependent random coil (1)H, (13)C, and (15)N chemical shifts of the ionizable amino acids: a guide for protein pK a measurements.Journal of biomolecular NMR · 2014Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
A NMR protocol is introduced that permits accurate measurement of minute, remote chemical shift perturbations (CSPs), caused by a mutation-induced change in the electric field. Using protein GB3 as a model system, (1)H(N) CSPs in K19A and K19E mutants can be fitted to small changes in the electric field at distal sites in the protein using the Buckingham equation, yielding an apparent dielectric constant εa of 8.6 ± 0.8 at 298 K. These CSPs, and their derived εa value, scale strongly with temperature. For example, CSPs at 313 K are about ∼30% smaller than those at 278 K, corresponding to an effective εa value of about 7.3 at 278 K and 10.5 at 313 K. Molecular dynamics simulations in explicit solvent indicate that solvent water makes a significant contribution to εa.
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Registered trials
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