- Email: firstname.lastname@example.org
- Thesis title: Novel Approaches to Proton Pumping Pyrophosphatases
- 2017 - present PhD: University of Leeds (UoL), UK
- 2014 - 2016 M.Sc. Biochemistry: Medical School Hannover (MHH), Germany
- 2011 - 2014 B.Sc. Biochemistry: Leibniz University Hannover (LUH), Germany
- 2003 - 2010 German "Abitur ", A-Levels (in Biology, Chemistry and Mathematics): Marie Curie Schule, Empelde (Germany)
- Jan 2017 - Jul 2017 Industrial Internship: Crystallography Department - Merck KGaA, Darmstadt (Germany)
- Oct 2015 - Feb 2016 Research Internship: Laboratory of Structural Biology – School of Biological Sciences, University of Auckland (New Zealand)
Integral membrane-bound pyrophosphatases (mPPases) couple the hydrolysis of pyrophosphate (PPi) to the generation of an electrochemical gradient by pumping H+ and/or Na+ ions across membranes. They are assigned to five different classes based on their pumping selectivity and requirement of K+ for maximal activity. mPPases are found in various prokaryotes, plants and protozoans and take part in plant maturation, bacterial stress resistance and the adoption of protozoan parasites to varying osmotic environments during their different stages of life. The absence of mPPases in humans and their important biological roles in several pathogens such as Trypanosoma brucei, Plasmodium falciparum and Bacteroides vulgatus make them a worthwhile target for structural studies supporting structure-guided drug design.
This PhD project is one of 12 in the EU network "Rationalising Membrane Protein crystallisation" (RAMP). RAMP is an Innovative Training Network (ITN) funded by the EU under a Marie Sklodowska Curie Action (MSCA). Other PhD students in network will work with other membrane proteins, develop advanced methods for crystallisation and modelling of the membrane protein crystallisation process.
The Project focuses on applying rational and novel crystallisation approaches to understand the mechanism of integral membrane pyrophosphatases. Lipidic cubic phase (LCP) crystallography will be explored to crystallise mPPases of unsolved classes. Later, time-resolved crystallography can be used to follow the enzymatic mechanism and neutron crystallography to identify proton positions. The work builds on recent papers of the Goldman group (Kellosaloet al. & Goldman.,Science 337, 473-476 (2012); Li et al. & Goldman, Nat Commun 7, 13596 (2016)) and involves secondments to other network partners with specialised crystallisation and crystallography expertise, such as Molecular Dimensions, the European Spallation Source and the Hamburg Centre for Ultrafast Imgaging.
RAMP-ITN website: https://ramp-itn.eu/