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Archiv-Übersicht     Angebot Nr. 13418

Angebotsdatum: 15. Mai 2019
Art der Stelle: Doktorarbeit
Fachgebiet: Chemie > Biochemie
Titel des Themas: Protein structural and functional dynamics using a combination of structural biology techniques, in particular NMR spectroscopy

Institut: Johannes Gutenberg-Universität Mainz, Inst. Pharmazie und Biochemie
Prof. Hellmich
JJ-Becherweg 30
55128 Mainz
Tel.:    Fax.:
Bundesland: Rheinland-Pfalz
Homepage: http://www.blogs.uni-mainz.de/fb09hellmich/membrane-biochemistry/
E-Mail Kontakt: mail

Beschreibung: The work group of Ute Hellmich (Inst. Biochemistry, Gutenberg University Mainz) is looking for a PhD student starting as soon as a suitable candidate is found. The position will be filled until March 2023 as a qualification for a PhD.

Project: Using a combination of solution NMR spectroscopy and other biophysical techniques (e.g. CD, EPR and fluorescence spectroscopy, ITC, SAXS, MS, X-ray crystallography and cryoEM) the successful candidate will investigate the structural and functional dynamics of essential human and pathogenic (bacterial and parasitic) proteins. For recent examples for our applications of an interdisciplinary research approach, please see e.g. Goretzki et al., 2018 Structure, or Wagner et al., 2019, Angewandte Chemie.
The work involves the cloning, overexpression and purification of proteins from bacterial and eukaryotic sources (E. coli, P. pastoris, T. brucei, Hek293 cells) and their functional and structural characterization, in particular protein-protein interaction as well as interactions between proteins and ligands such as inhibitors or lipids.
Our laboratory features a parasite (Trypanosoma brucei) and human cell culture, facilities for large scale preparative protein purification from bacterial and yeast sources and their functional and biophysical analysis. The lab is affiliated with the Centre for Biomolecular Magnetic Resonance (BMRZ), Goethe University Frankfurt where the NMR experiments will be carried out. For SAXS, EM and X-ray studies, the candidate may be expected to travel to synchrotron facilities and/or to spend some time (weeks to months) in a collaborator’s lab.
Candidates are required to have obtained a very good MSc in Biochemistry, Biophysics, Molecular Biology, Chemistry or closely related field. Fluency in English is required. Previous experience in molecular biology, cell culture, lipid biophysics and/or spectroscopy are a strong plus. Candidates with a background in (protein) NMR spectroscopy (e.g. from a MSc thesis) are especially encouraged to apply.
The successful applicant will carry out his/her work at Mainz University, Institute for Biochemistry but is expected to collaborate closely with the BMRZ in Frankfurt, which includes frequent travels to this site and participation in BMRZ workshops and seminars.
We offer a lively and friendly work environment and encourage interdisciplinary and collaborative work approaches. Lab languages are English and German. For more details, please visit our homepage:
Please send your applications with a CV, letter of motivation highlighting previous experience in protein biochemistry and structural biology, and the names of two individuals who will provide a letter of recommendation directly to Ute Hellmich u.hellmich@uni-mainz.de.
Methoden: - combination of solution NMR spectroscopy and other biophysical techniques (e.g. CD, EPR and fluorescence spectroscopy, ITC, SAXS, MS, X-ray crystallography and cryoEM)
- cell culture (human, parasitic)
- biochemistry, molecular biology (e.g. cloning, protein purification, functional assays)

Anfangsdatum: 15. Mai 2019
Geschätzte Dauer: 3.5 - 4 years
Papers: Wagner A, Le TA, Brennich M, Klein P, Bader N, Diehl E, Paszek D, Weickhmann AK, Dirdjaja N, Krauth-Siegel RL, Engels B, Opatz T, Schindelin H, Hellmich UA. (2019) Inhibitor-Induced Dimerization of an Essential Oxidoreductase from African Trypanosomes. Angew Chem Int Ed Engl. 258(11):3640-3644. doi: 10.1002/anie.201810470.

Goretzki B, Glogowski NA, Diehl E, Duchardt-Ferner E, Hacker C, Gaudet R, Hellmich UA. (2018) Structural Basis of TRPV4 N Terminus Interaction with Syndapin/PACSIN1-3 and PIP2. Structure. 26(12):1583-1593.e5. doi: 10.1016/j.str.2018.08.002.

Rose-Sperling D, Tran MA, Lauth LM, Goretzki B, Hellmich UA. (2019) 19F NMR as a versatile tool to study (membrane) protein structure and dynamics. Biol Chem. pii: /j/bchm.just-accepted/hsz-2018-0473/hsz-2018-0473.xml. doi: 10.1515/hsz-2018-0473. [Epub ahead of print]
Sonstiges: Candidates with a strong interest/background in (membrane) protein structural biology and protein dynamics are particularly encouraged to apply.