Carla Schmidt

studied Chemistry at the University of Leipzig, Germany, from 2001 to 2006. She performed her PhD work in the field of quantitative mass spectrometry at the Max Planck Institute for Biophysical Chemistry, Göttingen, Germany, and obtained her PhD in 2010 from the Georg August University Göttingen, Germany. In 2011, she moved to the University of Oxford, UK, to work with Carol Robinson in the field of structural mass spectrometry. Since 2016 she is a junior group leader and Junior Professor at the interdisciplinary research centre ZIK HALOmem at the MLU. Her research project focuses on the transient conformations of the intrinsically disordered synaptobrevin-2 and the factors that control disorder-to-order transitions.

Project within the RTG

The transient structures of intrinsically disordered synaptobrevin-2 as well as the structural elements formed in the presence of interaction partners will be explored by integrating cross-linking mass spectrometry, NMR spectroscopy and ion mobility-mass spectrometry with molecular dynamics simulations. The transition from the disordered to the ordered state will be followed and monitored.

Key publications

Liko I, Degiacomi MT, Mohammed S, Yoshikawa S, Schmidt C, Robinson CV. Dimer interface of bovine cytochrome c oxidase is influenced by local posttranslational modifications and lipid binding. Proc Natl Acad Sci USA. 2016, 113: 8230-8235.

Schmidt C, Robinson CV. A comparative cross-linking strategy to probe conformational changes in protein complexes. Nat Protoc. 2014, 9: 2224-2236.

Wittig S, Haupt C, Hoffmann W, Kostmann S, Pagel K, Schmidt C. Oligomerisation of Synaptobrevin-2 Studied by Native Mass Spectrometry and Chemical Cross-Linking. J Am Soc Mass Spectrom. 2019, 30: 149-160.

Website : https://www.halomem.de/en/research-group/#forschung