ArticleBiophysical journal2008
Is arginine charged in a membrane?
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 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.
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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
49 citing papers in PubMed, 87 citations in OpenAlex.
- Lipophilic mono-guanidinesRSC advances · 2026Article
- An innovative strategy to treat pathogenic biofilm-associated infectionsRSC medicinal chemistry · 2025Article
- Thermodynamics of arginine interactions with organic phosphates.Biophysical journal · 2025Article
- Ataxia-linked SLC1A3 mutations alter EAAT1 chloride channel activity and glial regulation of CNS function.The Journal of clinical investigation · 2022Article
- Functional Group Distributions, Partition Coefficients, and Resistance Factors in Lipid Bilayers Using Site Identification by Ligand Competitive Saturation.Journal of chemical theory and computation · 2021Article
- Aβ(1-42) tetramer and octamer structures reveal edge conductivity pores as a mechanism for membrane damage.Nature communications · 2020Article
- Breaking the Backbone: Central Arginine Residues Induce Membrane Exit and Helix Distortions within a Dynamic Membrane Peptide.The journal of physical chemistry. B · 2019Article
- Dynamic Protonation Dramatically Affects the Membrane Permeability of Drug-like Molecules.Journal of the American Chemical Society · 2019Article
- The importance of the membrane interface as the reference state for membrane protein stability.Biochimica et biophysica acta. Biomembranes · 2018Article
- Entropy and Polarity Control the Partition and Transportation of Drug-like Molecules in Biological Membrane.Scientific reports · 2017Article
- Preferential selection of Arginine at the lipid-water-interface of TRPV1 during vertebrate evolution correlates with its snorkeling behaviour and cholesterol interaction.Scientific reports · 2017Article
- Anhydrous Monoalkylguanidines in Aprotic and Nonpolar Solvents: Models for Deprotonated Arginine Side Chains in Membrane Environments.ACS omega · 2017Article
- Influence of High pH and Cholesterol on Single Arginine-Containing Transmembrane Peptide Helices.Biochemistry · 2016Article
- Ionization Properties of Histidine Residues in the Lipid Bilayer Membrane Environment.The Journal of biological chemistry · 2016Article
- Identification of the Fusion Peptide-Containing Region in Betacoronavirus Spike Glycoproteins.Journal of virology · 2016Article
- In silico prediction of drug therapy in catecholaminergic polymorphic ventricular tachycardia.The Journal of physiology · 2016Article
- Effect of methylation on the side-chain pKa value of arginine.Protein science : a publication of the Protein Society · 2016Article
- Transition State Charge Stabilization and Acid-Base Catalysis of mRNA Cleavage by the Endoribonuclease RelE.Biochemistry · 2015Article
- Membrane Protein Properties Revealed through Data-Rich Electrostatics Calculations.Structure (London, England : 1993) · 2015Article
- Constant-pH Molecular Dynamics Study of Kyotorphin in an Explicit Bilayer.Biophysical journal · 2015Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
"Charged" amino acids play countless important roles in protein structure and function. Yet when these side chains come into contact with membranes we do not fully understand their behavior. This is highlighted by a recent model of voltage-gated ion channel activity and translocon-based experiments that suggest small penalties to expose these side chains to lipids, opposing the prevailing view in membrane biophysics. Here we employ a side chain analog as well as a transmembrane helix model to determine the free energy as a function of protonation state and position for a lipid-exposed arginine (Arg) residue across a membrane. We observe high free energy barriers for both the charged and neutral states. Due to the stabilizing influence of membrane deformations for the protonated form, the Arg side chain experiences a pK(a) shift of <or=4.5 units and remains mostly protonated. The cost for exposing Arg to lipid hydrocarbon is prohibitively high with implications for many membrane translocating processes and the activation mechanisms of voltage-gated ion channels.
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What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.