Author

Sascha Lange

Leibniz-Forschungsinstitut für Molekulare Pharmakologie

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biophysics· 2 Molecular Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:protein folding & dynamics· 2 Research Focus:protein structure prediction· 2 Assay:cryo-EM· 1 Organism:E. coli· 1 Approach:microscopy & imaging analysis· 1 Assay:protein structure· 1 Assay:proteomics· 1

Frequent Co-Authors

Adam LangeiD· 3 shared Carl ÖsteriD· 3 shared Denis QorajiD· 3 shared Chaowei ShiiD· 2 shared Daniel RodereriD· 2 shared Han SuniD· 2 shared Shanshuang CheniD· 2 shared Taoran XiaoiD· 2 shared

Activity by Year

2025-2026 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 45 mutual co-author links

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3 shared papersBiophysics

Adam LangeORCID

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Author profile →

3 papers

Recent·Most cited

Atomic structure and plasticity of the MthK-CTX complex investigated by cryo-EM, NMR, and MD simulations

Denis Qoraj, Swantje Mohr, Ye. K. Aldakul, Thiemo Sprink, Carl Öster, Taoran Xiao, Peter Schmieder, Sascha Lange, Tillmann Utesch, Daniel Roderer, Shanshuang Chen, Han Sun, Adam Lange

The paper investigates the binding of scorpion toxin CTX to the MthK channel using cryo-EM, NMR, and MD simulations to explain toxin affinity and subtype tolerance.

Nature Communications · Aug 20, 2026Peer-reviewedMolecular Biology

Atomic structure and dynamics of the mechanosensitive channel MscL from E. coli by cryo-EM and solid-state NMR

Taoran Xiao, Alexandra Kovinko, Chaowei Shi, Henry Sawczyc, Denis Qoraj, Carl Öster, Thiemo Sprink, Sascha Lange, Spyridon Kosteletos, Han Sun, Daniel Roderer, Shanshuang Chen, Adam Lange

This study uses cryo-EM and solid-state NMR to determine the structure and dynamics of MscL from E. coli, revealing lipid-protein interactions that drive mechanosensitive gating.

bioRxiv · Apr 15, 2026 · PreprintBiophysics

Atomistic Mechanism of Calcium-Mediated Inward Rectification of the MthK Potassium Channel by Solid-State NMR and MD Simulations

Carl Öster, Reinier de Vries, Juan Li, Denis Qoraj, Sascha Lange, Chaowei Shi, Wojciech Kopeć, Bert L. de Groot, Adam Lange

This study identifies a calcium-mediated gating mechanism in the MthK potassium channel using solid-state NMR and MD simulations, revealing how Ca2+ blocks outward K+ flow while allowing inward flow.

Journal of the American Chemical Society · Dec 1, 2025Peer-reviewedBiophysics