SCIENCE-JOBS-DE

Cryo electron microscopy of amyloid oligomers

The research of the institute is on the structure and formation of amyloid fibrils and oligomers in disease. Amyloid oligomers from Aβ peptide are drivers of brain damage in Alzheimer’s disease and thus major health burdens and cost factors in aging Western societies. Obtaining more detailed structural data will important for improving our basic research understanding of the mechanism of fibril formation. In the long run, our work could form the basis of new diagnostic procedures or targeted intervention strategies.

Methoden:
Our new co-worker will further strengthen the research and teaching of our institute, carrying out a project that will use the Nobel Prize-winning method cryo electron microscopy (cryo-EM) to provide high resolution structural information about amyloid oligomers. Cryo-EM is an increasingly powerful tool to analyze the macromolecular structure of large biomolecules and will be the core technique to be applied here. The method involves a good deal of computational work, and the project additionally involves different methods of biochemical sample preparation and characterization.

Anfangsdatum: 2. November 2017

geschätzte Dauer: The position will be available immediately and will be initially limited to two years.

Bezahlung: TV-L  E13, 50%

Veröffentlichungen:
Cryo-EM reveals the steric zipper structure of a light chain-derived amyloid fibril. Schmidt A, Annamalai K, Schmidt M, Grigorieff N, Fändrich M Proc Natl Acad Sci U.S.A. 2016, 113, 6200-6205

Peptide Dimer Structure in an Aß(1-42) Fibril Visualized with Cryo-EM. Schmidt M, Rohou A, Lasker K, Yadav JK, Schiene-Fischer C, Fändrich M, Grigorieff N Proc Natl Acad Sci U.S.A. 2015, 112, 11858-11863

Structure and biomedical applications of amyloid oligomer nanoparticles. Kumar ST, Meinhardt J, Fuchs AK, Aumüller T, Leppert J, Büchele B, Knüpfer U, Ramachandran R, Yadav JK, Prell E, Morgado I, Ohlenschläger O, Horn U, Simmet T, Görlach M, Fändrich M ACS Nano 2014, 25, 8(11), 11042-52

Structural basis of Aβ-dependent synaptic dysfunctions. Christian Haupt C, Leppert J, Rönicke R, Meinhardt J, Yadav JK, Ramachandran R, Ohlenschläger O, Reymann KG, Görlach M, Fändrich M Angewandte Chemie Int. Edt. 2012, 51, 1576-1579

Solid-State NMR of Aβ Protofibrils Implies a β-Sheet Remodelling upon Maturation into Terminal Amyloid Fibrils. Scheidt HA, Morgado I, Rothemund S, Huster D, Fändrich M. Angewandte Chemie Int. Edt. 2011, 50, 2837 –2840

Homepage: http://https://www.uni-ulm.de/nawi/nawi-pbt.htm

Candidates for this project must hold a very good Master/Diplom degree in Biochemistry, Biophysics, Chemistry, Physics, Biology, Molecular Medicine or equivalent.  An application should consist of a completed questionnaire (for download under https://www.uni-ulm.de/fileadmin/website_uni_ulm/nawi.inst.206/Open_positions/Bewerberfragebogen_PhD.doc) a short cover letter, CV as well as transcripts of records from your Bachelor and Master courses preferably combined into one document/pdf-file (< 10 MB). Please submit your application, referring to “Amyloid oligomers”, to the following email address: bewerbung-pbc(at)uni-ulm.de. The position shall be filled a.s.a.p.. Please submit your application until 15 November 2017.

The Ulm University seeks to increase the number of women scientists and explicitly encourages qualified women to apply. Physically disabled applicants with equal qualifications will receive favorable consideration. The employment will be done by the central University administration.

* science-jobs-de sublist: SJD-BIOLOGY