Johannes Buchner

Molecular chaperones are an essential class of proteins that aid other proteins to obtain their biologically active structure and inhibit off-pathway side reactions during protein maturation.^[2] Buchner's work focuses on understanding mechanisms of molecular chaperones in a quantitative and mechanistic manner. His work has contributed to our understanding of the chaperone cycle of the bacterial chaperone GroEL^[3] and now lays a particular emphasis on small heat shock proteins (sHsps), the Hsp90 chaperone machinery and the role of molecular chaperones in antibody folding. Buchner's work established sHsps as molecular chaperones^[4] and has significantly contributed to our understanding of their function and mode of activation.^[5] His work on antibody folding delivered important insight in the mechanisms of how antibodies fold and are scrutinized by the cellular chaperone machinery.^[6] A major focus of Johannes Buchner's lab is the Hsp90 chaperone machine. His work has provided a detailed mechanistic understanding of Hsp90 and its regulation by co-chaperones, establishing a functional chaperone cycle for Hsp90, which has become a major target in cancer therapy^[7][8] Several discoveries from the Buchner lab on chaperone-mediated protein folding have been successfully translated into novel applications in biotechnology.

Buchner is a member of the Bavarian Academy of Sciences, the German Academy of Sciences and was from 2015 to 2016 president of the German Society for Biochemistry and Molecular Biology.^[9] Furthermore, he is a founding member of the Rainer Rudolph foundation. His work on protein folding and molecular chaperones has received several awards, among others the Hans Neurath Award of the Protein Society^[10] (2011), the Leopoldina Schleiden Medal (2015), the Albrecht-Kossel-Award (2016) and the Max Bergmann Medal (2017).