Cryo-EM structural analysis of amyloid fibrils

Prof M Fändrich
Dr Matthias Schmidt
Applications accepted all year round
Funded PhD Project (Students Worldwide)

Institute of Protein Biochemistry , University of Ulm

About This PhD Project

Project Description
Funding Notes
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References

Project Description

The Institute of Protein Biochemistry at Ulm University, Germany, investigates the molecular basis of amyloid diseases, such as Alzheimer’s disease and systemic amyloidosis. We use a broad range of techniques from protein biochemistry, structural biology (in particular cryo-EM) to cell biology. Our strong ties to several medical institutions enable us to uniquely link structural biology with patient samples.

We seek for several new doctorate students with an excellent Master degree in, for example, Biochemistry, Chemistry or Physics to strengthen our cryo-EM analysis of amyloid fibril structures. Projects may involve protein purification and sample preparation, cryo-EM imaging, computer-based single particle reconstruction, structural modelling and the combination of structural and biological/medical data.

Website: https://www.uni-ulm.de/nawi/nawi-pbc.html

Funding Notes

Several funded PhD positions are available or will become available at our institute in 2019. Please send an application consisting of cover letter, c.v. and certificates, preferably combined into one PDF document to the following email address bewerbung-pbc(at)uni-ulm.de. The position will initially be filled for 2 years with a possibility for an extension. Incoming mails will be viewed from 1 March 2019 onwards. Positions will be filled as soon as possible. Applications for self-funded projects are also welcome.

References

Cryo-EM structure of an amyloid fibril from systemic amyloidosis. Falk Liberta, Sarah Loerch, Matthies Rennegarbe, Angelika Schierhorn, Per Westermark, Gunilla T Westermark, Nikolaus Grigorieff, Marcus Fandrich, Matthias Schmidt, BioRxiv https://www.biorxiv.org/content/10.1101/357129v1

Physical basis of amyloid fibril polymorphism. Close W, Neumann M, Schmidt A, Hora M, Annamalai K, Schmidt M, Reif B, Schmidt V, Grigorieff N, Fändrich M. Nature Comm. 9, 699 (2018)

Common Fibril Structures Imply Systemically Conserved Protein Misfolding Pathways In Vivo. Annamalai K, Liberta F, Vielberg M-T, Close W, Lilie H, Gührs K-H, Schierhorn A, Koehler R, Schmidt A, Haupt C, Hegenbart U, Schönland S, Schmidt M, Groll M, Fändrich M Angew Chem Int Ed 56, 7618–7622 (2017)

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

Electron tomography reveals the fibril structure and lipid interactions in amyloid deposits. Kollmer M, Meinhardt K, Haupt C, Liberta F, Wulff M, Linder J, Handl L, Heinrich L, Loos C, Schmidt M, Syrovets T, Simmet T, Westermark P, Westermark GT, Horn U, Schmidt V, Walther P, Fändrich M. Proc Natl Acad Sci U.S.A. 2016, 113, 5604-5609

Polymorphism of amyloid fibrils in vivo. Annamalai K, Gührs KH, Koehler R, Schmidt M, Michel H, Loos C, Gaffney PM, Sigurdson CJ, Hegenbart U, Schönland S, Fändrich M Angewandte Chemie Int. Ed. 2016, 55, 4822–4825

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