05-Feb-2021 - Albert-Ludwigs-Universität Freiburg

Hierarchical dynamics

Researchers investigate signal transduction in proteins on many time scales

A tree moving in the wind: How long does it take for the movement of a branch to reach the tree trunk? And via which pathway is this movement transmitted? Researchers at Albert Ludwig University are applying these questions to proteins, the molecular machinery of the cell. A team led by Prof. Dr. Thorsten Hugel from the Institute of Physical Chemistry and Dr. Steffen Wolf and Prof. Dr. Gerhard Stock from the Institute of Physics is investigating how the signals that cause structural changes in proteins travel from one place to another and how quickly this happens. Since many time scales, from nanoseconds to seconds, are involved in such signal transduction, scientists have not yet been able to analyse the exact process. However, by combining different experiments, simulations and theoretical studies, the Freiburg researchers have now succeeded. They have published their results in the scientific journal Chemical Science.

In contrast to trees, movements of the Hsp90 protein investigated in the study occur on logarithmic time scales: Each larger movement takes about ten times as long as the small individual movements that make up the larger one. "For example, a branch would move every second, the branch every 10 seconds and the stem every 100 seconds," Wolf explained. The different methods of investigation allowed the researchers to describe an allosteric interaction, that is, to show how a reaction process in Hsp90 alters a distant protein-binding site. The team found that this allosteric process occurs via hierarchical dynamics that span time scales from nanoseconds to milliseconds and length scales from pico- to several nanometers, Stock said.

In addition, the reaction process in Hsp90 is coupled to a structural change in the single amino acid Arg380. Arg380, in turn, relays structural information to a subdomain of the protein and eventually to the entire protein. The resulting altered structure closes a central binding site of the protein, thereby enabling it to fulfil new functions. The Freiburg researchers assume that similar hierarchical mechanisms, such as the one found in the protein Hsp90, are also of fundamental importance in signal transduction in other proteins. This could be useful for the control of proteins by drugs, says Hugel.

Note: This article has been translated using a computer system without human intervention. LUMITOS offers these automatic translations to present a wider range of current news. Since this article has been translated with automatic translation, it is possible that it contains errors in vocabulary, syntax or grammar. The original article in German can be found here.

Facts, background information, dossiers

  • proteins

More about Uni Freiburg

  • News

    New discoveries about the origin of the brain’s immune system

    What gets into the brain and what doesn’t is strictly regulated. Researchers at the Faculty of Medicine at the University of Freiburg have now studied phagocytes that coat the blood vessels in the brain and reinforce the blood-brain barrier. As the scientists from the Institute of Neuropath ... more

    Lung Tissue from the Lab

    Laboratory studies of lung tissue usually require the removal of large amounts of human or animal tissue. Now scientists from the University of Freiburg’s Faculty of Medicine have succeeded in collaboration with American researchers in generating tiny quantities of lung tissue, so-called or ... more

    Complex pathways influence time delay in ionization of molecules

    How can researchers use the mechanism of photoionization to gain insight into complex molecular potential? This question has now been answered by a team led by Prof. Dr. Giuseppe Sansone from the Institute of Physics at the University of Freiburg. The researchers from Freiburg, the Max Plan ... more

  • q&more articles

    Modular biofactories at the cellular level

    Despite his love for complex molecular architectures, this „dyed-in-the-wool“ bio-organic chemist has never embraced the conventional segregation of synthetic polymers and bio­logical macromolecules. All molecules are composed of atoms, after all. Why make an artificial distinction? Why not ... more


    From a pluripotent stem cell a muscle cell or a liver cell can form, which despite their difference in appearance, are genetically identical. From one and the same genotype, therefore, the most diverse phenotypes can be formed – epigenetics is making it possible! It is a very exciting area ... more

  • Authors

    Dr. Stefan Schiller

    Stefan M. Schiller studied chemistry at Gießen (Mainz, Germany) and the University of Massachusetts, majoring in macromolecular chemistry and biochemistry. For his doctorate in biomimetic membrane systems he worked till 2003 at the Max Planck Institute for Polymer Research in Mainz. Researc ... more

    Julia M. Wagner

    Julia M. Wagner studied pharmacy in Freiburg (licensure 2008). Since 2008 she is a PhD student and research assistant in the group of Professor Dr. M. Jung. Her research focuses ­on the cellular effects of histone deacetylase inhibitors. more

    Prof. Dr. Manfred Jung

    Manfred Jung is a graduate of the University of Marburg, where he studied pharmacy (licensure  1990) and obtained his doctorate in pharmaceutical chemistry with Prof. Dr. W. Hanefeld. After a post-doctorate at the University of Ottawa, Canada, he began with independent research in 1994 ­at ... more

q&more – the networking platform for quality excellence in lab and process

The q&more concept is to increase the visibility of recent research and innovative solutions, and support the exchange of knowledge. In the broad spectrum of subjects covered, the focus is on achieving maximum quality in highly innovative sectors. As a modern knowledge platform, q&more offers market participants one-of-a-kind networking opportunities. Cutting-edge research is presented by authors of international repute. Attractively presented in a high-quality context, and published in German and English, the original articles introduce new concepts and highlight unconventional solution strategies.

> more about q&more

q&more is supported by: