Healthcare industry

Three researchers at the MPI for Immunobiology and Epigenetics receive millions in funding from the European Research Council. Dominic Grün, Nicola Iovino and Ritwick Sawarkar from the Max Planck Institute of Immunobiology and Epigenetics in Freiburg will each be awareded one of the prestigious Consolidator Grants of the European Research Council. This means that 6 million euros in funding will go to fundamental research in Freiburg over the next…

Article - 02/08/2016

Can the ticking Huntington clock be stopped?

An early phase clinical study involving thirty-six Huntington’s disease (HD) patients is currently underway to investigate whether a method called gene silencing can cure the disease. If the gene that causes the disease can be turned off, it would be the first step towards a treatment that not only fights symptoms but actually treats the causes of HD, hence providing a cure.

Article - 12/05/2016

Novel method for predicting the spatial structure of biomolecules

Biomolecules can only fulfil their functions in the cell when they fold into a characteristic native three-dimensional structure. Knowing this structure is not only of paramount importance for basic research, but also for medicine and pharmacology. Scientists from the Karlsruhe Institute of Technology (KIT) have therefore developed a simple method to predict the three-dimensional structure of biomolecules from the analysis of readily available…

Article - 07/03/2016

Looking at the control of cellular homeostasis

Many biological processes that occur in our body are driven and controlled by protein complexes. In order to better understand these processes, biochemist Prof. Dr. Florian Stengel from the University of Konstanz is developing methods that will eventually make it possible to study the architecture, interactions and general dynamics of intact protein complexes quantitatively and in detail. Stengel combines structural mass spectrometry methods with…

Article - 03/11/2014

Dementia and the prion principle

Prions are misfolded proteins that are associated with diseases such as BSE, Creutzfeldt-Jakob disease and scrapie. What makes prions particularly dangerous is their ability to induce properly folded proteins to convert into misfolded prion forms. This principle seems to be more widespread than previously thought. Dr. Mathias Jucker from the University of Tübingen and his American colleague Lary Walker from Emory University have put forward a…

Article - 29/09/2014

Andrei Lupas – fascination for the complex world of proteins

Prof. Dr. Andrei Lupas is a molecular biologist and director of the Department of Protein Evolution at the Max Planck Institute (MPI) for Developmental Biology in Tübingen. He became fascinated by the incredible complexity of proteins early on during his scientific career. His work focuses on the use of laboratory and computational methods to solve the question as to how a simple amino acid chain becomes a protein ‘nanomachine’. Lupas and his…

Article - 19/05/2014

Computational chemistry as atomistic magnifying glass for biological systems

Studying biological macromolecules such as proteins in their entirety on the atomistic level is a huge experimental challenge. Prof. Dr. Christine Peter from the University of Konstanz is therefore working on the development of special computer models that are able to calculate and visualize the complex interaction of atoms. She is using these models to study the chemical basis of complex biological phenomena such as protein folding and the…

Article - 05/05/2014

Magnetic amino acids for measuring proteins

Dr. Malte Drescher and Dr. Daniel Summerer, two chemists from Konstanz University, have developed an innovative method for studying protein structures using magnetic labels inside cells. The method is based on non-canonical magnetic amino acids that are directly incorporated into the protein as it is biosynthesised in the cell. A patent has been filed for the method, which could potentially lead to major progress in the field of structural…

Article - 26/08/2013

Like a bridge of molecules

Proteins are the active part of cells. They recognise sequences transport nutrients and information as well as getting rid of waste. Proteins that go from one side of a membrane through to the other serve as transporters and channels and help molecules across membranes. Dr. Thomas Becker and his colleagues from the Institute for Biochemistry and Molecular Biology at the University of Freiburg are studying these complex processes. They are…

Article - 05/08/2013

Marina Rubini – a passionate researcher into protein folding and design

Therapeutic proteins play an important role in modern medicine. Correct glycosylation patterns are therefore fundamentally important for producing effective glycoprotein-based therapeutics. Dr. Marina Rubini from the University of Konstanz explores ways to alter the properties of proteins using non-natural amino acids for the post-translational site-specific attachment of carbohydrate groups. She uses the glycoprotein hormone erythropoietin…

Article - 22/07/2013

Marcus Fändrich strengthens protein biochemistry at Ulm University

After quite a long vacancy the directors post of the Institute for Pharmaceutical Biotechnology at the University of Ulm has finally been filled. Marcus Fändrich and his team moved into the laboratories and offices of the new life sciences building on the Oberer Eselsberg Ulm University campus in November 2012. Fändrich fills a gap in the Ulm Bioregions biopharmaceutical education activities as he will not only be teaching biochemistry…

Article - 04/03/2013

Protein folding to unravel the origin of life

Computer analyses of protein folding have shed light on the evolution of early life on earth. Researchers from the Heidelberg Institute for Theoretical Studies and the University of Illinois, USA, have examined the folding speed of the domains of proteins and found that there has been a trend towards the optimisation of protein folding since their appearance 3.8 billion years ago. 1.5 billion years ago, more complex domain structures and…

Press release - 27/08/2012

New insights to the Function of Molecular Chaperones

Heidelberg molecular biologists have gained new insights into the function of so-called molecular chaperones in protein synthesis. The team headed by Dr. Günter Kramer and Prof. Dr. Bernd Bukau of the DKFZ-ZMBH Alliance was able to demonstrate how a molecular chaperone in bacterial cells can influence the formation of the three-dimensional structure of new proteins.

Article - 07/11/2011

Martin van der Laan and the labyrinth inside mitochondria

Mitochondria contain an intertwined membrane system that is necessary for the production of energy. Errors in the inner mitochondrial membrane architecture prevent energy from being produced. A group of researchers led by Dr. Martin van der Laan at the University of Freiburg in cooperation with partners has identified a protein complex that plays a key role in the architecture and functioning of the mitochondria.

Article - 12/09/2011

How snails can survive heat

Professor Dr. Heinz-R. Köhler and Professor Dr. Rita Triebskorn two zoologists from the University of Tübingen are working with research teams from Avignon Esslingen Gießen and Le Havre to investigate how snails are able to adapt to extreme climatic conditions on the molecular cellular and physiological level. Their Hot Snail project is funded by the German Research Foundation DFG and its particular objective is to find out whether reactions to…

Article - 10/01/2011

Review: What does the cell factory of the future look like?

A symposium on “Cell Factories of the Future” was held at the Laupheim-based company Rentschler Biotechnologie on 14th and 15th October 2010. The event attracted around 70 scientists from academia and industry and will now take place every two years. The symposium focused on new biomanufacturing developments and technologies, and included lectures on (animal) cells, cell factories and the future of recombinant protein production.

Article - 09/08/2010

Quick and early detection of rare diseases

Lysosomal storage diseases LSD are a group of around 50 rare inherited metabolic disorders. Only 12 LSDs have been described biochemically and microbiologically. Prof. Dr. Michael Przybylski from the Steinbeis Transfer Centre for Biopolymer Analysis and Proteomics at the University of Constance now hopes to change this situation. In a project carried out in cooperation with the biotech company Genzyme CEE Konstanz and the University of Timisoara…

Article - 15/07/2010

A special focus on intercellular mediators

Transmembrane proteins constitute around one third of all cellular proteins. Around half of all drugs that are currently on the market target the function of a specific class of transmembrane proteins, i.e. the G-protein coupled receptors. However, little is yet known about how transmembrane proteins are integrated into the membranes and how they are folded. Dr. Jörg H. Kleinschmidt hopes to shed light into the mechanisms of membrane protein…

Article - 30/11/2009

The problem children of protein biochemistry

A large number of cellular proteins are located in or on a membrane. Dr. Dirk Schneider from the University of Freiburg believes that biochemists who investigate such proteins must be a little crazy, as the methods required to isolate the molecules from their exotic environment, i.e. from the lipid bilayer, are extremely difficult and complicated. Research has long focused on water-soluble proteins. Schneider and his team have now taken on the…

Article - 10/09/2009

Chaperone research using baker’s yeast and bacteria

Protein misfolding and aggregation can lead to neurodegenerative diseases such as Alzheimers. Prof. Elke Deuerling at the University of Constance is investigating the molecular helpers the chaperones and the key role that they have in protein folding. Deuerling uses the bakers yeast Saccharomyces cerevisiae and the bacterium Eschericia coli for her studies. Her studies involving E. coli have now shown that ribosome-associated chaperones are…

Prof. Bernd Bukaus team from the Centre for Molecular Biology at the University of Heidelberg has succeeded for the very first time in gaining an understanding of the molecular mechanisms that enable cells to dissolve stress-related protein aggregates.

Article - 06/04/2008

Molecular chaperons in algal chloroplasts

Michael Schroda from the Department of Plant Biochemistry at the University of Freiburg is examining the role of HSP70B a chaperon in the chloroplasts of Chlamydomonas reinhardtii algae which is important for protecting the algae against high light intensity.

Holger Barth works with a special kind of Trojan horses. The toxicologist from Ulm is investigating bacterial toxins. These proteins manage in a similar way to the ancient Greeks before them to open the barricaded portal of the cells with a trick whereupon they start wreaking destruction.