ArticleChemical communications (Cambridge, England)2017
Determining rotational dynamics of the guanidino group of arginine side chains in proteins by carbon-detected NMR.
Article in Chemical communications (Cambridge, England), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 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
14 citing papers in PubMed.
- Arginine: I. Interactions of Its Guanidinium Moiety with Branched Aliphatic Side Chains.The journal of physical chemistry. B · 2025Article
- A pH-Centric Model of Nucleolar Activity and Regulation.Journal of molecular biology · 2025Review
- Slow Rotational Dynamics of Cytosine NHBiochemistry · 2022Article
- Review
- Hindered Rotations of Protein Asparagine/Glutamine Side-Chain NHThe journal of physical chemistry letters · 2021Article
- Multiquantum Chemical Exchange Saturation Transfer NMR to Quantify Symmetrical Exchange: Application to Rotational Dynamics of the Guanidinium Group in Arginine Side Chains.The journal of physical chemistry letters · 2020Article
- Mass spectrometry assisted arginine side chains assignment of NMR resonances in natural abundance proteins.Journal of biomolecular NMR · 2020Article
- Characterising side chains in large proteins by protonlessNature communications · 2019Article
- Dynamic ion pair behavior stabilizes single α-helices in proteins.The Journal of biological chemistry · 2019Article
- The pKProtein science : a publication of the Protein Society · 2019Article
- Arginine Side-Chain Hydrogen Exchange: Quantifying Arginine Side-Chain Interactions in Solution.Chemphyschem : a European journal of chemical physics and physical chemistry · 2019Article
- NMR Methods for Characterizing the Basic Side Chains of Proteins: Electrostatic Interactions, Hydrogen Bonds, and Conformational Dynamics.Methods in enzymology · 2019Review
- Impact of two-bondJournal of biomolecular NMR · 2018Article
- AJournal of biomolecular NMR · 2017Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Arginine residues are imperative for many active sites and protein-interaction interfaces. A new NMR-based method is presented to determine the rotational dynamics around the N
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Registered trials
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