ArticleProteins2011
Histidine in continuum electrostatics protonation state calculations.
Article in Proteins, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 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
6 citing papers in PubMed.
- Charge Neutralization During Peptide Transport in the Bacterial SecYEG Translocon.Biomolecules · 2025Article
- Significance of Histidine Hydrogen-Deuterium Exchange Mass Spectrometry in Protein Structural Biology.Biology · 2024Review
- A comprehensive analysis of the computed tautomer fractions of the imidazole ring of histidines in Loligo vulgaris.Journal of biomolecular structure & dynamics · 2018Article
- Energy Minimization of Discrete Protein Titration State Models Using Graph Theory.The journal of physical chemistry. B · 2016Article
- Proteins as strongly correlated protonic systems.FEBS letters · 2012Review
- Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
A modification to the standard continuum electrostatics approach to calculate protein pK(a)s, which allows for the decoupling of histidine tautomers within a two-state model, is presented. Histidine with four intrinsically coupled protonation states cannot be easily incorporated into a two-state formalism, because the interaction between the two protonatable sites of the imidazole ring is not purely electrostatic. The presented treatment, based on a single approximation of the interrelation between histidine's charge states, allows for a natural separation of the two protonatable sites associated with the imidazole ring as well as the inclusion of all protonation states within the calculation.
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Registered trials
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