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Archiv-Übersicht     Angebot Nr. 13856

Angebotsdatum: 8. April 2020
Art der Stelle: Doktorarbeit
Fachgebiet: Chemie > Biochemie
Titel des Themas: 2 PhD Positions at TU Berlin in Antibiotic Mode of Action and Antibiotic Resistance

Institut: Institut für Chemie/Biologische Chemie
Prof. Roderich Süßmuth
10623 Berlin
Tel.:    Fax.:
Homepage: http://www.biochemie.tu-berlin.de/Research/ResearchHome.xhtml
E-Mail Kontakt: mail

Beschreibung: 2 PhD Positions in Antibiotic Mode of Action and Antibiotic Resistance: Biochemistry/Structural Biology, Süßmuth group, Institute of Chemistry, Technische Universität Berlin, Germany

The Technische Universität Berlin continually ranks among the top academic institutions of the world and is one of the leading research institutions in Germany. The university provides an exceptionally diverse research environment enabling interdisciplinary collaborations by bringing together technical subjects with the humanities, economics, and social and planning sciences. The campus is located close to Tiergarten and Zoologischer Garten in the centre of Berlin, close to cafes, restaurants, shopping areas and parks.

Applications are invited for a PhD candidate position, which is available immediately or upon mutual agreement. The goal of the projects is the characterization of interactions between bioactive molecules and their cellular targets by a combination of biophysical and molecular biological techniques. The successful candidate (m/f/d) will have a keen interest in structural biology (NMR spectroscopy and/or X-ray crystallography) and interdisciplinary collaborative research, ideally with a strong background in molecular biology, (protein-)biochemistry and biophysics. If you love science, are self-motivated with a strong desire to understand how antibiotics work on a molecular level, this could be the right PhD for you!

The Süßmuth group at TU Berlin offers an exciting interdisciplinary research environment with excellent facilities including protein purification laboratories, several in-house NMR and Mass-Spec instruments. Our group specializes in the chemical synthesis of natural products, as well as investigating their biosynthetic pathways, mode of action and resistance mechanisms. For more details see our group homepage (https://www.biochemie.tu-berlin.de/Research/ResearchHome.xhtml).
The group is involved in collaborations with industry, research groups from other Universities and the Institute of Chemistry itself. The proximity of several (bio-)medical and pharmacological research institutions in Berlin (Charité, Forschungsinstitut für Molekulare Pharmakologie, Max Delbrück Center for Molecular Medicine etc.) enables students and researchers to work in a unique collaborative environment.

PhD candidates (m/f/d) will hold (or expect to complete soon) an excellent M.Sc. (or equivalent) degree in (bio-)chemistry, molecular biology, biophysics or a related field. The group language is English, so no German language skills are required – but it’s a great opportunity for you to learn German.

Interested? Submit your application including cover letter (explaining background and motivation), CV, transcripts (including university entrance degree), and the contact details of at least one person who would be willing to provide a letter of reference, preferably via e-mail as one single PDF file to:
Methoden: Cloning, gene expression and purification of protein constructs
Mass spectrometry (HPLC-ESI-MS/-MS2, MALDI-MS)
X-ray crystallography
Biomolecular NMR spectroscopy
(Cryo-) Electron microscopy
Circular dichroism spectroscopy, Isothermal titration calorimetry, etc..
Bioinformatic tools
Anfangsdatum: 1. Juni 2020
Geschätzte Dauer: 3-4 Jahre
Papers: Molecular insights into antibiotic resistance - how a binding protein traps albicidin.
Rostock, L., Driller, R., Grätz, S., Kerwat, D., von Eckardstein, L., Petras, D., Kunert, M., Alings, C., Schmitt, F.-J., Friedrich, T., Wahl, M.C., Loll, B., Mainz, A., Süssmuth*, R.D.
Nat. Commun. 2018, 9(1), 3095

The anti-staphylococcal lipolanthines are ribosomally synthesized lipopeptides.
Wiebach, V., Mainz, A., Siegert, M.-A.J., Jungmann, N.A., Lesquame, G., Tirat, S., Dreux-Zigha, A., Aszodi, J., Le Beller, D., Süssmuth*, R.D.
Nat. Chem. Biol. 2018, 14(7), 652-654

The Albicidin resistance factor AlbD is a serine endopeptidase that hydrolyzes unusual oligoaromatic-type peptides.
Vieweg, L., Kretz, J., Pesic, A., Kerwat, D., Grätz, S., Royer M., Cociancich, S., Mainz, A., Süssmuth*, R.D.
J. Am. Chem. Soc. 2015, 137(24), 7608-7611

The gyrase inhibitor albicidin consists of p-aminobenzoic acids and cyanoalanine.
Cociancich, S., Pesic, D., Petras, D., Uhlmann, S., Kretz, J., Schubert, V., Vieweg, L., Duplan, S., Marguerettaz, M., Noell, J., Pieretti, I.,
Hügelland, M., Kemper, S., Mainz, A., Rott, P., Royer*, M., Süssmuth*, R.D.
Nat. Chem. Biol. 2015, 11(3), 195-197