ReviewCurrent opinion in structural biology2026
High-speed atomic force microscopy of membrane proteins: From dynamic imaging to integrative structural biology.
Review in Current opinion in structural biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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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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Authors and funding
3 authors.
Funding
Abstract
High-speed atomic force microscopy (HS-AFM) enables direct, label-free visualization of membrane proteins in lipid bilayers with nanometer spatial resolution and millisecond temporal resolution. Recent studies revealed transient conformational states, dynamic oligomerization changes, and membrane-mediated organization of membrane proteins that are not readily captured by conventional structural or biophysical approaches. Advances in experimental design-including membrane reconstitution strategies, stimulus-coupled imaging, high-temporal-resolution acquisition, and computational reconstruction-have further expanded the scope of HS-AFM. When integrated with complementary techniques such as cryo-electron microscopy, molecular dynamics simulations, and single-molecule methods, HS-AFM provides a powerful and versatile tool for linking membrane protein structure, dynamics, and function in native-like environments.
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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.