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Profile

The biogenesis and degradation of proteins are facilitated by macromolecular interactions, which are difficult to study structurally due to their transient nature. Our aim is to obtain structural insights into synthesis and post-translational modification of secretory proteins as well as protein degradation by the ubiquitin-proteasome system using integrative approaches. We use cryoelectron tomography (CET) to unravel ER-associated processes in situ, at this point primarily protein import into the ER, and we develop and apply computational procedures for extensive data mining of volumetric data. The structure of the 26S proteasome is studied on the atomic level using computational approaches that integrate subnanometer cryo-EM reconstructions and interaction data. 

 
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