Press releases - News from the MPI of Biochemistry

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Getting even closer to the limit

August 20, 2018
Ralf Jungmann, Research Group Leader at the MPI of Biochemistry and Professor at the LMU in Munich, demonstrates in a pioneering study together with his team, the potential of modified aptamers in super-resolution fluorescence microscopy. Their results were published in the journal Nature Methods. [more]
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The “TRiC” to folding actin

August 09, 2018
Proteins must be folded correctly to fulfill their molecular functions in cells. Molecular assistants called chaperones help proteins exploit their inbuilt folding potential and reach the correct three-dimensional structure. Researchers at the Max Planck Institute of Biochemistry (MPIB) have demonstrated that actin, the most abundant protein in higher developed cells, does not have the inbuilt potential to fold and instead requires special assistance to fold into its active state. The chaperone TRiC uses a previously undescribed mechanism to perform actin folding. The study was recently published in the journal Cell. [more]
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Three ERC Starting Grants for Group Leaders at the MPIB

July 27, 2018
The European Research Council (ERC) encourages excellent research in Europe to promote visionary projects and open up new interdisciplinary science areas. Three young research group leaders at the Max Planck Institute of Biochemistry (MPIB) in Martinsried near Munich succeeded in obtaining one of the coveted “ERC Starting Grants”. Out of more than 3100 applications, only 403 researchers were selected in this year’s competition. Spread over a period of five years, Hannes Mutschler, Danny Nedialkova, and Karl Duderstadt will receive up to € 1.5 million each for their research on fundamental questions of life. [more]
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Crowd Control

July 02, 2018
Have you ever been stuck in the middle of a crowd? As people pack closer together, it becomes more difficult to move through the crowd. Sometimes it can become so tightly packed that you cannot move at all. If this sounds uncomfortable, then you probably wouldn’t like to live inside a cell, which is densely packed with proteins and other molecules. This crowding is very important for the cell—it pushes the molecules together so that they can interact and perform the chemical reactions that the cell needs to live. In fact, many human diseases are likely influenced by changes in molecular crowding that cause harmful interactions between proteins. Despite its importance, it remains a mystery how the crowding inside cells is controlled. Combining biophysics, cell biology, physical modeling, and cryo-electron tomography, an international team of scientists at New York University (NYU) and the Max Plank Institute of Biochemistry (MPIB) has discovered that the mTORC1 signaling pathway controls the concentration of ribosomes inside the cell, thereby regulating crowding and the ability of proteins to interact with each other to form phase-separated compartments. This study is published in the journal Cell. [more]
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Finding the off-switch for side effects

June 21, 2018
Opioids are powerful painkillers that act on the brain, but they have a range of harmful side effects including addiction. Researchers have developed a tool that gives deeper insights into the brain’s response to opioids. Using mass spectrometry, they determined changes of proteins’ phosphorylation patterns – the molecular switches of the proteins – in five different regions of the brain and assigned them to the desired and the undesired effects of opioid treatment. Their results, which are published in the journal Science, will lead the way for the identification of novel drug targets and the design of a new class of painkillers with fewer side effects. The study was performed by researchers at the Max Planck Institute of Biochemistry (MPIB) in collaboration with researchers from the Medical University of Innsbruck, Austria, University of Innsbruck, and Temple University, USA. [more]
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Tag it EASI – a new method for accurate protein analysis

June 18, 2018
Protein analysis is becoming an increasingly important tool on the road towards personalized medicine. The method of choice for this purpose is mass spectrometry. Scientists at the Max Planck Institute of Biochemistry have developed a new labelling method for proteins called EASI-Tag. The new method makes it possible to analyze multiple samples at the same time using conventional mass spectrometers. Unlike earlier approaches, EASI-Tag is able to detect quantitative differences between samples extremely accurately. The method has now been presented in the scientific journal Nature Methods. [more]
 
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