ArticleNano letters2015
High-speed AFM images of thermal motion provide stiffness map of interfacial membrane protein moieties.
Article in Nano letters, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- High-Speed Atomic Force Microscopy Reveals the Dynamic Interplay of Membrane Proteins is Lipid-Modulated.Small science · 2025Article
- Antithetic effects of agonists and antagonists on the structural fluctuations of TRPV1 channel.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Hybridization of papain molecules and DNA-wrapped single-walled carbon nanotubes evaluated by atomic force microscopy in fluids.Scientific reports · 2023Article
- Multiple pore lining residues modulate water permeability of GlpF.Protein science : a publication of the Protein Society · 2022Article
- CRISPR/Cas9 Genome Editing vs. Over-Expression for Fluorescent Extracellular Vesicle-Labeling: A Quantitative Analysis.International journal of molecular sciences · 2021Article
- ScatteringNanoscale advances · 2021Article
- Label-free characterization of an extracellular vesicle-based therapeutic.Journal of extracellular vesicles · 2021Article
- Cell Surface Binding and Lipid Interactions behind Chemotherapy-Drug-Induced Ion Pore Formation in Membranes.Membranes · 2021Article
- Localization atomic force microscopy.Nature · 2021Article
- DNA origami demonstrate the unique stimulatory power of single pMHCs as T cell antigens.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Native-like membrane models of E. coli polar lipid extract shed light on the importance of lipid composition complexity.BMC biology · 2021Article
- Biological physics by high-speed atomic force microscopy.Philosophical transactions. Series A, Mathematical, physical, and engineering sciences · 2020Review
- Interaction of the motor protein SecA and the bacterial protein translocation channel SecYEG in the absence of ATP.Nanoscale advances · 2020Article
- Visualization of Single Molecules Building a Viral Capsid Protein Lattice through Stochastic Pathways.ACS nano · 2020Article
- Article
- Review
- Single-file transport of water through membrane channels.Faraday discussions · 2018Article
- Quantification of Water Flux in Vesicular Systems.Scientific reports · 2018Article
- Directly watching biomolecules in action by high-speed atomic force microscopy.Biophysical reviews · 2017Review
- Imaging modes of atomic force microscopy for application in molecular and cell biology.Nature nanotechnology · 2017Review
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
The flexibilities of extracellular loops determine ligand binding and activation of membrane receptors. Arising from fluctuations in inter- and intraproteinaceous interactions, flexibility manifests in thermal motion. Here we demonstrate that quantitative flexibility values can be extracted from directly imaging the thermal motion of membrane protein moieties using high-speed atomic force microscopy (HS-AFM). Stiffness maps of the main periplasmic loops of single reconstituted water channels (AqpZ, GlpF) revealed the spatial and temporal organization of loop-stabilizing intraproteinaceous H-bonds and salt bridges.
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