ArticleProceedings of the National Academy of Sciences of the United States of America2013
Hydration dynamics as an intrinsic ruler for refining protein structure at lipid membrane interfaces.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed.
- A water-pinning hotspot drives templated tau aggregation.bioRxiv : the preprint server for biology · 2026Article
- Peptides display multilayered hydration shell substructures dictated by sequence-specific surface chemistry.Nature communications · 2026Article
- Physical and Mechanical Properties of Monomeric Alpha-Synuclein Provide Leads to Molecular Function.The journal of physical chemistry. B · 2025Article
- Solution-like Water Transport Across Molecular to Macroscopic Length Scales in Crosslinked Poly(ethylene glycol diacrylate) Networks with Tailored Sidechains.Journal of polymer science (2020) · 2025Article
- Water-directed pinning is key to tau prion formation.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Exploring the influence of water micro assemblies on protein folding, enzyme catalysis and membrane dynamics.European biophysics journal : EBJ · 2025Review
- Spin-labeling Insights into How Chemical Fixation Impacts Glycan Organization on Cells.Applied magnetic resonance · 2024Article
- α-Synuclein and biological membranes: the danger of loving too much.Chemical communications (Cambridge, England) · 2023Review
- Investigating water/oil interfaces with opto-thermophoresis.Nature communications · 2022Article
- Plasticity of Membrane Binding by the Central Region of α-Synuclein.Frontiers in molecular biosciences · 2022Article
- The docking of synaptic vesicles on the presynaptic membrane induced by α-synuclein is modulated by lipid composition.Nature communications · 2021Article
- Missense Mutations Modify the Conformational Ensemble of theFrontiers in molecular biosciences · 2021Article
- An Emerging Role for Phosphoinositides in the Pathophysiology of Parkinson's Disease.Journal of Parkinson's disease · 2021Review
- Electrostatic Environment of Proteorhodopsin Affects the pKa of Its Buried Primary Proton Acceptor.Biophysical journal · 2020Article
- High-resolution Overhauser dynamic nuclear polarization enhanced proton NMR spectroscopy at low magnetic fields.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2020Article
- Ultrafast Dynamics of Water-Protein Coupled Motions around the Surface of Eye Crystallin.Journal of the American Chemical Society · 2020Article
- Soluble endogenous oligomeric α-synuclein species in neurodegenerative diseases: Expression, spreading, and cross-talk.Journal of Parkinson's disease · 2020Review
- Parkinson's disease: proteinopathy or lipidopathy?NPJ Parkinson's disease · 2020Review
- A Role of Cholesterol in Modulating the Binding of α-Synuclein to Synaptic-Like Vesicles.Frontiers in neuroscience · 2020Article
- Dynamic behaviors of α-synuclein and tau in the cellular context: New mechanistic insights and therapeutic opportunities in neurodegeneration.Neurobiology of disease · 2019Review
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Authors and funding
5 authors.
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Abstract
Knowing the topology and location of protein segments at water-membrane interfaces is critical for rationalizing their functions, but their characterization is challenging under physiological conditions. Here, we debut a unique spectroscopic approach by using the hydration dynamics gradient found across the phospholipid bilayer as an intrinsic ruler for determining the topology, immersion depth, and orientation of protein segments in lipid membranes, particularly at water-membrane interfaces. This is achieved through the site-specific quantification of translational diffusion of hydration water using an emerging tool, (1)H Overhauser dynamic nuclear polarization (ODNP)-enhanced NMR relaxometry. ODNP confirms that the membrane-bound region of α-synuclein (αS), an amyloid protein known to insert an amphipathic α-helix into negatively charged phospholipid membranes, forms an extended α-helix parallel to the membrane surface. We extend the current knowledge by showing that residues 90-96 of bound αS, which is a transition segment that links the α-helix and the C terminus, adopt a larger loop than an idealized α-helix. The unstructured C terminus gradually threads through the surface hydration layers of lipid membranes, with the beginning portion residing within 5-15 Å above the phosphate level, and only the very end of C terminus surveying bulk water. Remarkably, the intrinsic hydration dynamics gradient along the bilayer normal extends to 20-30 Å above the phosphate level, as demonstrated with a peripheral membrane protein, annexin B12. ODNP offers the opportunity to reveal previously unresolvable structure and location of protein segments well above the lipid phosphate, whose structure and dynamics critically contribute to the understanding of functional versatility of membrane proteins.
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