High-speed atomic force microscopy of membrane and membrane protein dynamics

High-speed atomic force microscopy (HS-AFM) enables direct nanometer-resolution visualization of single molecules and molecular assemblies in real-time and under physiological conditions, providing unique insights into how membranes and membrane proteins move and interact within native lipid environments. Recent methodological advances and integration with complementary techniques have extended HS-AFM to increasingly complex, physiologically relevant systems, bridging gaps between high-resolution static structural methods and low-resolution functional dynamics. Here, we highlight how HS-AFM has changed our understanding of membrane organization, protein conformational dynamics, and lipid-protein coupling. By capturing transient events inaccessible to ensemble approaches, HS-AFM is transforming our ability to connect structural snapshots with functional behavior, advancing dynamic structural biology.

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Publication Details

Journal
Current Opinion in Structural Biology
Published
2026-05-30
DOI
https://doi.org/10.1016/j.sbi.2026.103294
Primary Topic
Force Microscopy Techniques and Applications
Type
article
Field-Weighted Citation Impact
0.00

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article

High-speed atomic force microscopy of membrane and membrane protein dynamics

George R. Heath, Bashra Mahamed, Abeer Alshammari
Current Opinion in Structural Biology
Force Microscopy Techniques and Applications
article

High-speed atomic force microscopy of membrane and membrane protein dynamics

George R. Heath, Bashra Mahamed, Abeer Alshammari
article en

Abstract

High-speed atomic force microscopy (HS-AFM) enables direct nanometer-resolution visualization of single molecules and molecular assemblies in real-time and under physiological conditions, providing unique insights into how membranes and membrane proteins move and interact within native lipid environments. Recent methodological advances and integration with complementary techniques have extended HS-AFM to increasingly complex, physiologically relevant systems, bridging gaps between high-resolution static structural methods and low-resolution functional dynamics. Here, we highlight how HS-AFM has changed our understanding of membrane organization, protein conformational dynamics, and lipid-protein coupling. By capturing transient events inaccessible to ensemble approaches, HS-AFM is transforming our ability to connect structural snapshots with functional behavior, advancing dynamic structural biology.

Current Opinion in Structural BiologyVol. 99
University of Leeds (GB), University of Hafr Al-Batin (SA)
Engineering and Physical Sciences Research Council
Openalex Percentile: Top 5%
Force Microscopy Techniques and Applications
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