PhD students wanted! 

(June 2026)

We are looking for 2 motivated PhD students 

1) NMR characterization of the protein misfolding and aggregation  
We aim to better understand the structural mechanism that underlies protein aggregation and amyloid formation. In particular, we investigate small molecules, chaperones, and cellular components such as glycosaminoglycans that influence the aggregation behaviour and effect amyloid fibril structure and cellular toxicity. Protein systems under investigation involve the Alzheimer’s disease Aβ peptide, the diabetes type II related human islet amyloid polypeptide (hIAPP), light chain antibody domains involved in AL-amyloidosis and serum amyloid A (SAA) involved in AA-amyloidosis. We employ solution- and MAS solid-state NMR to characterize these systems. In addition, we use low resolution biophysical methods such as fluorescence microscopy, ThT aggregation assays, CD spectroscopy, negative-stain EM and DLS.

2) MAS solid-state NMR methods 
Solid-state NMR experiments are intrinsically insensitive due to orientation dependent anisotropic interactions. In addition, the applied rf fields are time dependent due to sample rotation. Optimum control derived strategies allow to overcome this problem and increase the sensitivity of each magnetization transfer step significantly. It will be aim of the PhD project to implement the concept of sensitivity improvement by exploiting coherence order selection in homo- and heteronuclear triple resonance rf pulse schemes to yield sequential backbone assignments. 

Our group is integrated into the Bavarian NMR Center (www.bnmrz.org) and is associated with the Institute of Structural Biology (www.helmholtz-munich.de/en/stb) at the Helmholtz-Zentrum München. 

If you are interested, please send an email to reif@tum.de.

References 
Tošner Z, Brandl MJ, Blahut J, Glaser SJ, Reif B (2021) Maximizing efficiency of dipolar recoupling in solid-state NMR using optimal control sequences. Sci. Adv. 7: eabj5913; doi: 10.1126/sciadv.abj5913.
Blahut J, Brandl MJ, Pradhan T, Reif B, Tosner Z (2022) Sensitivity-Enhanced Multidimensional Solid-State NMR Spectroscopy by Optimal-Control-Based Transverse Mixing Sequences. J. Am. Chem. Soc. 144: 17336-17340; doi: 10.1021/jacs.2c06568.
Pradhan T, Sarkar R, Meighen-Berger KM, Feige MJ, Zacharias M, Reif B (2023) Mechanistic insights into the aggregation pathway of the patient-derived immunoglobulin light chain protein FOR005. Nat. Commun. 14: e3755; doi: 10.1038/s41467-023-39280-0.
Rodina N, Hornung S, Sarkar R, Suladze S, Peters C, Schmid PWN, Niu Z, Haslbeck M, Buchner J, Kapurniotu A, Reif B (2024) Modulation of Alzheimer's Disease Aβ40 Fibril Polymorphism by the Small Heat Shock Protein αB-Crystallin. J. Am. Chem. Soc. 146, 19077; doi: 10.1021/jacs.4c03504.
Suladze S, Sarkar R, Rodina N, Bokvist K, Krewinkel M, Scheps D, Nagel N, Bardiaux B, Reif B (2024) Atomic resolution structure of full- length human insulin fibrils. Proc. Natl. Acad. Sci. USA 121, e2401458121; doi: 10.1073/pnas.2401458121.
Suladze S, Sustay Martinez C, Rodriguez Camargo DC, Engler J, Rodina N, Sarkar R, Zacharias M, Reif B (2024) Structural Insights into Seeding Mechanisms of hIAPP Fibril Formation. J. Am. Chem. Soc. 146, 13783; doi: 10.1021/jacs.3c14233.