ArticleThe journal of physical chemistry. B2010
Water-protein interactions of an arginine-rich membrane peptide in lipid bilayers investigated by solid-state nuclear magnetic resonance spectroscopy.
Article in The journal of physical chemistry. B, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 82 citations in OpenAlex.
- Harnessing Membrane-Active Peptides for Selective Cancer Targeting: Phosphatidylserine Recognition by Tilapia Piscidin 4.JACS Au · 2026Article
- In Silico Modelling of the AQP0 T138R Mutation and its' links to Potential Mechanisms of Cataractogenesis.Research square · 2025Article
- Solid state NMR spectral editing of histidine, arginine and lysine using Hadamard encoding.Journal of biomolecular NMR · 2025Article
- Water Accessibility Refinement of the Extended Structure of KirBac1.1 in the Closed State.Frontiers in molecular biosciences · 2021Article
- Hydration and Dynamics of Full-Length Tau Amyloid Fibrils Investigated by Solid-State Nuclear Magnetic Resonance.Biochemistry · 2020Article
- Role of Membrane Potential on Entry of Cell-Penetrating Peptide Transportan 10 into Single Vesicles.Biophysical journal · 2020Article
- Influence of Lipid Saturation, Hydrophobic Length and Cholesterol on Double-Arginine-Containing Helical Peptides in Bilayer Membranes.Chembiochem : a European journal of chemical biology · 2019Article
- Enhancement of exfoliating efficacy of L-carnitine with ion-pair method monitored by nuclear magnetic resonance spectroscopy.Scientific reports · 2019Article
- Gradients in Wall Mechanics and Polysaccharides along Growing Inflorescence Stems.Plant physiology · 2017Article
- Icephobic Surfaces Induced by Interfacial Nonfrozen Water.ACS applied materials & interfaces · 2017Article
- Mapping protein-protein interactions by double-REDOR-filtered magic angle spinning NMR spectroscopy.Journal of biomolecular NMR · 2017Article
- Structural biology of supramolecular assemblies by magic-angle spinning NMR spectroscopy.Quarterly reviews of biophysics · 2017Review
- Probing Hydronium Ion Histidine NH Exchange Rate Constants in the M2 Channel via Indirect Observation of Dipolar-DephasedJournal of the American Chemical Society · 2016Article
- Atomic-resolution structure of the CAP-Gly domain of dynactin on polymeric microtubules determined by magic angle spinning NMR spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- (15)N and (1)H Solid-State NMR Investigation of a Canonical Low-Barrier Hydrogen-Bond Compound: 1,8-Bis(dimethylamino)naphthalene.The journal of physical chemistry. B · 2015Article
- Cellulose-Pectin Spatial Contacts Are Inherent to Never-Dried Arabidopsis Primary Cell Walls: Evidence from Solid-State Nuclear Magnetic Resonance.Plant physiology · 2015Article
- Investigating Hydrophilic Pores in Model Lipid Bilayers Using Molecular Simulations: Correlating Bilayer Properties with Pore-Formation Thermodynamics.Langmuir : the ACS journal of surfaces and colloids · 2015Article
- Article
- Probing membrane protein structure using water polarization transfer solid-state NMR.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2014Article
- Characterization of the water defect at the HIV-1 gp41 membrane spanning domain in bilayers with and without cholesterol using molecular simulations.Biochimica et biophysica acta · 2014Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The interaction of an arginine (Arg) residue with water in a transmembrane antimicrobial peptide, PG-1, is investigated by two-dimensional heteronuclear correlation (HETCOR), solid-state nuclear magnetic resonance (NMR) spectroscopy. Using (13)C and (15)N dipolar-edited (1)H-(15)N HETCOR experiments, we unambiguously assigned a water-guanidinium cross-peak that is distinct from intramolecular protein-protein cross-peaks. This water-Arg cross-peak was detected within a short (1)H spin diffusion mixing time of 1 ms, indicating that water is in close contact with the membrane-inserted guanidinium. Together with previously observed short guanidinium-phosphate distances, these solid-state NMR data suggest that the Arg side chains of PG-1 are stabilized by both hydration water and neutralizing lipid headgroups. The membrane deformation that occurs when water and lipid headgroups are pulled into the hydrophobic region of the bilayer is symptomatic of the membrane-disruptive function of this antimicrobial peptide. The water-Arg interactions observed here provide direct experimental evidence for molecular dynamics simulations of the solvation of Arg side chains of membrane proteins by deeply embedded water in lipid bilayers.
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