Max Planck Institute of Biophysics

A new study reveals the dual role of MLKL in necroptosis, paving the way for new treatments for inflammatory diseases.

A new structural study reveals the mechanism used by anaerobic microbes to grow on a mixture of carbon dioxide and other gases

Researchers have a better understanding of how our cells dispose of waste while developing ways to control it

Dynamic structure of FLVCR proteins and their function in nutrient transport in our cells revealed

Claire Donnelly and Eugene Kim will receive the 2024 Heinz Maier-Leibnitz Prize of the German Research Foundation

It can take hours and hours to solve a puzzle with a thousand pieces. It tookv Martin Beck from the Max Planck Institute of Biophysics in Frankfurt 20 years to complete a very special puzzle: the researcher and his team uncovered the arrangement of the thousand protein molecules that make up each nuclear pore – protein complexes that form a tunnel-like passage through the membrane of the cell nucleus. The proteins serve as both gates and gatekeepers: they connect the nucleus with the surrounding cell and actively control what is allowed in and out. Viruses, for example, have to remain outside.

Talking with friends, enjoying a concert, talking on the phone on noisy streets – people with hearing problems are often unable to hear things that others can. Tobias Moser aims to make sound accessible to those with hearing disabilities in a whole new way through a new generation of hearing protheses. Known as optical cochlear implants, these devices serve as an example of therapies developed on the basis of fundamental research.

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.

Have you ever pulled a loop out of entangled cables, resulting in even more knots? A true safeguard in our body, the protein Smc5/6, can do this without creating an inextricable mess. It helps to store our meter-long DNA free of knots in the tiny nuclei of our cells and to maintain the integrity of our genes by forming DNA loops. If Smc5/6 makes a mistake, our genetic material can be damaged. Such defects can lead to rare hereditary diseases, developmental disorders or cancer. Understanding how Smc5/6 functions helps us to identify new target points for medical therapies.

As control units of our cells, nuclei contain and guard our genetic material. Pores in the nuclear membrane form the only gateway in and out of the nucleus, allowing important messenger molecules to pass but blocking dangerous invaders such as pathogens. They thus help the nucleus to communicate with the rest of the cell while protecting the genetic material. Such challenging task requires a complex biological structure that has kept many scientists occupied for over two decades; a jigsaw puzzle with missing pieces that we could now solve to near completion.

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.

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.

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.