Manajit Hayer-Hartl

Dr. Manajit Hayer-Hartl is a Professor and Group Leader at the Max Planck Institute of Biochemistry in Martinsried, Germany, where she heads the Research Group 'Chaperonin-Mediated Protein Folding' within the Department of Cellular Biochemistry. She has held a W2 Professor position at the Max Planck Society since 2019, following her Minerva Program position (2014-2019), and has been an Independent Research Group Leader since 2006.

Her research focuses on understanding how molecular chaperones assist in protein folding and assembly, with particular emphasis on the chaperonin system GroEL-GroES and its role in folding complex proteins like Rubisco. Her groundbreaking work has solved the longstanding challenge of producing functional Rubisco (the key protein of photosynthesis with 16 subunits) in vitro using chaperones and helper proteins. Her laboratory employs biochemical and biophysical techniques including single molecule FRET and hydrogen-deuterium exchange coupled to mass spectrometry to investigate conformational transitions during protein folding.

Dr. Hayer-Hartl's research has significant implications for understanding fundamental biological processes and potentially improving photosynthetic efficiency in plants, which could enhance crop performance and help address climate change through increased CO₂ fixation. Her publications primarily focus on chaperonin mechanisms, protein folding dynamics, and the assembly of complex protein structures like Rubisco.

• Major Awards:
• Merck Award of ASBMB (2020)
• Elected Member, Leopoldina Academy (2018)
• Charles F. Kettering Award (2018)
• Dorothy Crowfoot Hodgkin Award (2017)
• Elected Member, EMBO (2016)

As a mentor, Dr. Hayer-Hartl supervises PhD students and postdoctoral researchers, including Alonso Izzat Carvajal Alvarez. Her laboratory collaborates extensively within the Department of Cellular Biochemistry, working closely with other research groups studying molecular chaperones and protein homeostasis. The research group utilizes advanced mass spectrometry facilities including an LTQ FT mass spectrometer and Waters Synapt HDMS system for proteomics applications and structural analysis of protein complexes.