Department News

Researchers at the Max Planck Institute of Biochemistry (MPIB) have identified a novel mechanism that ensures proteostasis maintenance in E. coli when chaperone availability is limited. more

Researchers at the Max Planck Institute of Biochemistry decipher the molecular mechanism of Rubisco activase in a recent study more

Brenda Schulman, Ulrich Hartl and Wolfgang Baumeister receive a research grant to study Mechanisms of Parkinsons’s disease more

Researchers for protein folding helpers at the Max Planck Institute of Biochemistry have now deciphered the molecular structure of the EL phage chaperonin and discovered special features. more

The biochemist Hartl and the geneticist Horwich are honored with the world’s highest science prize for their groundbreaking discovery of the protein folding, assistans, chaperones. more

The nucleolus is a well-known cellular structure that is easily visible under a light microscope. This nuclear structure is known as the site of ribosome production. In a recent study, researchers at the Max Planck Institute of Biochemistry in Martinsried, Germany, have shown that the nucleolus is also a site of quality control for proteins. When cells are stressed, proteins tend to misfold and to aggregate. To prevent proteins from clumping, some are temporarily stored in the nucleolus. The special biophysical conditions found in this organelle prevent harmful protein aggregation. The results of this study have now been published in the journal Science. more

F.-Ulrich Hartl, Director at the Max Planck Institute of Biochemistry, and Arthur Horwich of Yale School of Medicine and Howard Hughes Medical Institute were named winners of the 2019 Dr. Paul Janssen Award for Biomedical Research. Selected by an independent committee of world-renowned scientists, Hartl and Horwich won for their revolutionary insights into chaperone-mediated protein folding. Hartl expresses his delight to have been selected as one of the winners of the Dr. Paul Janssen Award. “This is a fantastic honor and recognition of the work of my laboratory”, he says. The award includes a $200,000 prize and will be presented at ceremonies in the USA and Belgium in September. more

F.-Ulrich Hartl, Director at the Max Planck Institute of Biochemistry in Martinsried near Munich, is awarded the Paul Ehrlich- and Ludwig Darmstaedter-Prize 2019 together with Arthur L. Horwich.  of Yale School of Medicine/HHMI.The biochemist Hartl and the geneticist Horwich are honored for their pioneering work in the field of cellular protein chemistry. Their collaboration helped unravel the molecular machinery that assists protein folding. The prize will be awarded on March 14 in the St. Paul‘s Church in Frankfurt and is endowed with 120,000 EUR. more

F.-Ulrich Hartl, director at the Max Planck Institute of Biochemistry in Martinsried, was inducted into the Hall of Fame of German Research. The award, which was introduced by the Manager Magazin in 2009, honors Hartl as a pioneer in the field of cellular biochemistry. Together with colleagues in the USA, Hartl demonstrated that newly produced proteins do not fold spontaneously but require the assistance by folding helpers, so called chaperones. This finding refuted the central dogma that proteins in cells can fold spontaneously, just as they do in the test tube. Hartl’s research shows that misfolded proteins contribute to neurodegenerative diseases like Alzheimer’s and Parkinson’s disease and are associated with malfunction of chaperones.   more

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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