Max Planck Institute of Biophysics

Max Planck Institute of Biophysics

At the Max Planck Institute of Biophysics, research is mainly focused on proteins that are embedded in or associated with biological membranes. Among other things, membrane proteins act as channels, transporters or molecular sensors for the exchange of substances and information between the cell and its environment, but they are also important for transport within cells. The Institute's scientists use electron microscopy and X-ray crystallography to analyse the structure of these proteins. In an ideal complement to the experimental investigations, these molecular processes are also modelled in the computer, in order to describe them quantitatively and gain a detailed understanding of the underlying mechanisms.

Contact

Max-von-Laue-Straße 3
60438 Frankfurt am Main
Phone: +49 69 6303-0
Fax: +49 69 6303-4502

PhD opportunities

This institute has no International Max Planck Research School (IMPRS).

There is always the possibility to do a PhD. Please contact the directors or research group leaders at the Institute.

<strong>Water exchange in magnesium’s hydration shells impacts biological processes</strong>

Atomistic insights into the exchange dynamics on the millisecond timescale from transition path sampling

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<p>Enzyme catalysis by selective compression of bulky ring-shaped substrates</p>

The hydride transfer between methylene-tetrahydromethanopterin and NADP+

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The spikes of the virus crown

Max Planck researchers want to analyse the surface protein of the coronavirus to identify binding sites for vaccines and drugs

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<p>Muscle cells need calcium ions</p>

Structural analysis for a ryanodine receptor 1 gain insight into calcium release during muscle contraction

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Custom-Tailored Molecules

4/2014 Biology & Medicine

Chlamydomonas reinhardtii, a single-celled green alga, can’t see much at all with its eye composed solely of photosensitive rhodopsin molecules. Yet there is more to algal rhodopsin than one would expect. In recent years, it has triggered a revolution in neurobiology. Ernst Bamberg from the Max Planck Institute of Biophysics in Frankfurt helped make it famous. He is now researching these molecules and developing new variants for basic research and medical applications.

Peter Mombaerts is as familiar with the world of molecules, genes and cellular signals as he is with the world of odors. The Belgian, who is now Director at the Max Planck Institute of Biophysics in Frankfurt/Main, is one of the researchers who have clarified what pathway odors take through the nose and brain – or at least the basic principles of it.

No job offers available

Electron cryo-microscopy of membrane protein complexes

2019 Kühlbrandt, Werner

Structural Biology

Single-particle electron cryo-microscopy (CryoEM) is ideal for determining the high-resolution structure membrane protein complexes that are too unstable or too dynamic for x-ray crystallography. Intact rotary ATPases have resisted crystallization for more than 40 years. However, central aspects of their mechanisms now have become clear thanks to the recent CryoEM based structures of intact, functional ATP synthases. The two best and most informative of these structures, the chloroplast ATP synthase and a mitochondrial ATP synthase dimer, have been shown by our department.

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Acyl-CoA dehydrogenase/electron-transferring flavoprotein complexes: Structural determinants of a flavin-based electron bifurcation

2018 Kayastha, Kanwal; Demmer, Julius K.; Müller, Volker; Buckel, Wolfgang; Ermler, Ulrich

Cell Biology

Flavin-based electron bifurcating (FBEB) enzyme complexes play a vital role in obligate anaerobic microorganisms for increasing the efficiency of their energy metabolism. They drive an endergonic reduction by an exergonic one via the same electron donor. The energy coupling is realized by a reduced flavin which transfers via energy splitting one strongly and one weakly reducing electron to two different substrates. How FBEB enzyme complexes are structurally constructed is outlined using the example of two acyl-CoA dehydrogenase/electron-transferring flavoproteins.

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Molecular mechanisms of lipid membrane shaping and quality control

2017 Hummer, Gerhard

Cell Biology Structural Biology

Living cells are coated and structured by lipid membranes. We addressed two important questions: how are membranes shaped into their often unusual forms, and how do cells monitor the membrane state? With molecular and coarse-grained simulations, we could show how the proteins Mga2 and Ire1 can sense the state of the endoplasmic reticulum. Also, new insights have been obtained about the fusion of vesicles, the formation of tubular structures in the endoplasmic reticulum, and the induction of autophagosomes aided by the Atg1 complex.

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Structure of dimeric ATP synthase from the inner membrane of yeast mitochondria

2016 Hahn, Alexander; Parey, Kristian; Bublitz, Maike; Mills, Deryck J.; Zickermann, Volker; Vonck, Janet; Kühlbrandt, Werner; Meier, Thomas

Cell Biology Structural Biology

We determined the structure of a complete, dimeric F1Fo-ATP synthase from mitochondria of the yeast Yarrowia lipolytica by a combination of cryo-electron microscopy (cryo-EM) and X-ray crystallography. The structure resolves 58 of the 60 subunits in the dimer. Horizontal helices of subunit a in Fo wrap around the c-ring rotor, and a total of six vertical helices assigned to subunits a, b, f, i, and 8 span the membrane. Our data explain the structural basis of cristae formation in mitochondria, a landmark signature of eukaryotic cell morphology.

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How nature reduces molecular oxygen to water conserving energy at the same time

2015 Michel, Hartmut; Ermler, Ulrich; Safarian, Schara

Structural Biology

Molecular oxygen appeared in the atmosphere about three billion years ago. Nature developed two membrane integrated enzymatic systems which reduce oxygen to water and use the energy of this reaction to produce biologically important energy carriers. These enzymes are the haem-copper terminal oxidases, e.g. cytochrome c oxidase, and the bd oxidases. The atomic structures of representative members of both enzyme families were determined. These evolutionary unrelated enzymes apparently use the same mechanisms to conserve energy and to prevent the formation of toxic reactive oxygen species.

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