Welcome to the Max Planck Institute of Biophysics!

Welcome to the Max Planck Institute of Biophysics!

We study the structure and function of proteins which regulate vital cellular processes using a wide methodological repertoire including advanced light and electron microscopy and as well as computational biology.

Our Research


Werner Kühlbrandt – Structural Biology
Gerhard Hummer – Theoretical Biophysics
Ana J. García-Sáez
Ulrich Ermler – Enzyme Mechanism
Martin Beck – Molecular Sociology
Ernst Bamberg – The Functional Analysis of Electrogenic Membrane Proteins
Eugene Kim – Structure and Dynamics of Chromosomes
Melanie McDowell – Membrane Protein Biogenesis
Hartmut Michel – Molecular Membrane Biology
Bonnie Murphy – Redox and Metalloproteins
Beata Turoňová – Image Processing
Florian Wilfling – Mechanisms of Cellular Quality Control

Overview

Scientific Facilities


Sonja Welsch – Electron Microscopy
Julian Langer – Mass Spectrometry
https://brain.mpg.de/imaging

News

Abstract representation of a cell undergoing ferroptosis with a central blue shape, encircled by green dots, and outer red membrane resembling petals.

Shining a New Light on Ferroptosis

Research News
Researchers at the Max Planck Institute of Biophysics and the University of Cologne developed a new optical tool to study ferroptosis, a form of iron-driven cell death. Better understanding of how it spreads could open doors to new therapies.
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Girls’ Day on April 3, 2025

Girls’ Day on April 3, 2025

Events Upcoming Events
Be a scientist for a day! Solve biological 3D puzzles and discover how tiny building blocks control your body!
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Understand what we do

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Meet us

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Work with us

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Latest Publications

1.
Ros, U.; Martinez-Osorio, V.; Valiente, P. A.; Abdelwahab, Y.; Gojkovic, M.; Shalaby, R.; Zanna, S.; Saggau, J.; Wachsmuth, L.; Nemade, H. N. et al.; Zoeller, J.; Lottermoser, H.; Chen, Y.-G.; Ibrahim, M.; Kelepouras, K.; Vasilikos, L.; Bedoya, P.; Espiritu, R. A.; Müller, S.; Altmannova, V.; Tieleman, D. P.; Weir, J.; Langer, J. D.; Adam, M.; Walczak, H.; Wong, W. W.-L.; Liccardi, G.; Mollenhauer, M.; Pasparakis, M.; Peltzer, N.; García-Sáez, A. J.: MLKL activity requires a splicing-regulated, druggable intramolecular interaction. Molecular Cell 85 (2025)
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2.
Taniguchi, R.; Orniacki, C.; Kreysing, J. P.; Zila, V.; Zimmerli, C. E.; Böhm, S.; Turoňová, B.; Kräusslich, H.-G.; Doye, V.; Beck, M.: Nuclear pores safeguard the integrity of the nuclear envelope. Nature Cell Biology (2025)
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3.
Zabelskii, D.; Bukhdruker, S.; Bukhalovich, S.; Tsybrov, F.; Lamm, G. H. U.; Astashkin, R.; Doroginin, D.; Matveev, G.; Sudarev, V.; Kuzmin, A. et al.; Zinovev, E.; Vlasova, A.; Ryzhykau, Y.; Ilyinsky, N.; Gushchin, I.; Bourenkov, G.; Alekseev, A.; Round, A.; Wachtveitl, J.; Bamberg, E.; Gordeliy, V.: Ion-conducting and gating molecular mechanisms of channelrhodopsin revealed by true-atomic-resolution structures of open and closed states. Nature Structural & Molecular Biology (2025)
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4.
Fuchs, J.; Fernández-Arévalo, U.; Demmer, U.; Díaz, E.; Ullmann, G. M.; Pierik, A. J.; Ermler, U.; Boll, M.: Enzymatic Birch reduction via hydrogen atom transfer at [4Fe-4S]-OH2 and [8Fe-9S] clusters. Nature Communications 16, 3236 (2025)
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