High-Speed AFM and Cryo-EM: Dynamics and Structures of Membrane Proteins
January 27, 2026 @ 15:15 – 16:15 CET
Simon Scheuring
Weill Cornell Medicine, USA
Simon Scheuring is Distinguished Professor of Anesthesiology Research in the Department of Anesthesiology at Weill Cornell Medicine in New York, USA.
He is a trained biologist (Biozentrum, University of Basel, Switzerland). During his MSc and PhD, he learned electron microscopy (EM) and atomic force microscopy (AFM) for the structure determination of membrane proteins such as aquaporins and sugar transporters. During his postdoc and as research assistant (Institut Curie, Paris, France), he learned membrane physical chemistry and developed AFM for the study of native membranes and ventured into setting up his lab as a junior research director at the Institut Curie. Promoted to senior research director, he built a larger laboratory in Marseille (INSERM / Aix-Marseille Université, France). In 2017, he moved to Weill Cornell Medicine, where he got appointed as Professor in the Department of Anesthesiology (WCM, New York, USA). Simon Scheuring’s laboratory develops and applies AFM-technologies for the study of membrane phenomena, such as membrane protein structure, assembly, diffusion, and conformational dynamics of unlabeled single molecules, bridging structure and function. Over the past years, his laboratory has been instrumental in the development of High-Speed AFM (HS-AFM) methods, extracting quasi-atomic structural details from single molecule AFM data, and reaching millisecond temporal resolution for the analysis of conformational dynamics. In recent works, his laboratory combines HS-AFM with cryo-EM to acquire an integrated understanding of the dynamics and structures of membrane proteins.
Abstract
High-speed atomic force microscopy (HS-AFM) is a powerful technique that provides dynamic movies of biomolecules at work. First, I will briefly review our recent developments to break temporal limitations to characterize molecular dynamics by developing HS-AFM line scanning (HS-AFM-LS) and HS-AFM height spectroscopy (HS-AFM-HS) [1], and resolution limitations by developing Localization AFM (LAFM) [2]. Then, I will detail how we used HS-AFM to analyze membrane-embedded TRPV3 at the single-molecule level, and discovered a previously unobserved, transient, and reversible pentameric state of TRPV3, while cryo-EM analysis allowed to resolve the first structure of a pentameric TRP channel [3,4]. Finally, I will report about our most recent efforts to develop and apply 3D-AFM for the characterization of the water structure on protein surfaces [5].
References:
[1] Heath et al., Nature Communications, 2018, 9(1):4983, High-Speed AFM Height Spectroscopy (HS-AFM-HS): Microsecond dynamics of unlabeled biomolecules.
[2] Heath et al., Nature, 2021, 594(7863):385–390, doi:10.1038/s41586-021-03551-x, Localization Atomic Force Microscopy.
[3] Lansky et al., Nature, 2023, 621(7977), 206–214, doi:10.1038/s41586-023-06470-1, A pentameric TRPV3 channel with a dilated pore.
[4] Lansky et al. Nature Communications, 2025, 16(4520). https://doi.org/10.1038/s41467-025-59798-9, Structural dynamics and permeability of the TRPV3 pentamer. [5] Ma et al., submitted, 2025, Aquaporins destructure water above the pore.
Host: Stavros Azinas stavros.azinas@scilifelab.se
Google Calendar 
