Rate My Professor Sebastian Hiller

Hiller's research group specializes in structural biology and biophysics, utilizing solution nuclear magnetic resonance (NMR) spectroscopy and complementary methods to elucidate the atomic-resolution structures, dynamics, and functions of proteins and their interaction partners. Central themes encompass the principles of chaperone function through analysis of chaperone-client complexes implicated in neurodegenerative diseases like Parkinson’s disease; the biogenesis of bacterial outer membrane proteins, including mechanisms of the insertase BamA and development of antibiotics such as darobactin and OMPTA; and the conformational dynamics of kinases regulated by second messengers in bacteria alongside interactions in the mammalian TOR complex governing cell growth. The group has produced landmark publications including "Structure of the NINJ1 filament" (Nature, 2023), "Mode of action of darobactin" (Nature, 2021), "Activation of translation in eukaryotes" (Molecular Cell, 2021), "Interaction of molecular chaperones with α-synuclein" (Nature, 2020), and highly cited works such as "GSDMD membrane pore formation constitutes the mechanism of pyroptotic cell death" (EMBO Journal, 2016), "A new antibiotic selectively kills Gram-negative pathogens" (Nature, 2019), and "Solution structure of the integral human membrane protein VDAC-1 in detergent micelles" (Science, 2008). Hiller has garnered prestigious accolades, including the 2018 ICMRBS Founder’s Medal for pioneering NMR applications in protein structure and function, the 2014 EMBO Young Investigator award, the 2011 ERC Starting Grant, the 2010 SNSF Professorship, and the 2008 SNSF Scholarship for young researchers. He is listed among the world’s most highly cited researchers.