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Postdoc Position Biophysics

Postdoc Position
Postdoc Position (E13/TV-L Biophysics): Protein aggregation and fibril formation: From bulk solution and cosolvents to the living cell

The Cluster of Excellence RESOLV (Ruhr Explores Solvation; www.ruhr-uni-bochum.de/solvation) announces a post­doc­to­ral position in the field of Solvation Science. RESOLV is funded within the German Excellence Initiative and aims at establishing „Solvation Science“ as an overarching research topic at RUB. The mission of RESOLV is to launch Solvation Science as a new interdisciplinary field to understand the influence of solvation on reactions, the function of bio­mo­le­cules, and processes at liquid-solid interfaces. RESOLV aims to create an interdisciplinary framework for understanding solvent processes that is universal and adds a predictive capability.

This interdisciplinary research project aims to understand the molecular principles of protein aggregation and fibril for­ma­tion as a cause of neurodegenerative disease. We are looking for an enthusiastic and highly motivated individual in­ter­es­ted in interdisciplinary techniques and innovative methods to study protein aggregation in vitro, in cellulo and in vivo. The researcher will be embedded in RESOLV's international research environment working with the groups of Prof. R. Winter (TU, Dortmund) and Jun.-Prof. S. Ebbinghaus (RU Bochum).

Information about the groups can be found at: www.chemie.tu-dortmund.de/winter/ and www.rub.de/pc2/ebbinghaus

Applicants require a Ph.D. in biophysics or a related fields. The position is funded for 2 years.

Project description:
A wide range of proteins are known to form aggregates and amyloids upon misfolding and aggregation, causing neu­ro­de­ge­ne­ra­tive diseases like Alzheimer or Chorea Huntington. Despite recent experimental and theoretical advances used to understand protein ag­gre­ga­tion and fibrillation processes, the underlying mechanisms of protein solvation versus ag­gre­ga­tion have proven to be challenging to study. The effects of co-solvents, crowding and confinement conditions on ag­gre­ga­tion and fibrillation phenomena of proteins are still largely unknown and have only reached a phenomenological level of understanding so far, without the ability to describe their role in the living cell. The observed coincidence of amyloid-related diseases with the patients' age suggests that some extra- and intracellular factors, including natural osmolytes, may escape mechanisms of physiological regulation at an old age, and play a role in triggering the disease. For example, glycerol and trimethylamine N-oxide (TMAO), which normally rectify folding defects in proteins, are capable of inducing aggregation of Alzheimer β-peptide. Hence, the role of hydrational forces in protein aggregation and their modulation by co-solvents, crowding effects and the presence of lipid interfaces attracts considerable interest and is instrumental in elucidating the molecular basis of amyloidosis and cellular toxicity. The postdoctoral research project aims to understand solvent and co-solvent effects that prevent or trigger protein aggregation in the living cell. The goal is to increase the complexity of the solvent to mimic the cellular environment, finally being able to interpret in-cell studies.

Application:
Applications should include a detailed curriculum vitae (with information about awards and presentations), and a list of all publications. The Ruhr Universität Bochum is committed to employ more handicapped individuals and especially en­cou­rages them to apply. The RUB wishes to increase the share of women in areas, where they are underrepresented and strongly encourages them to apply.

Please email (as a single pdf-file) your application no later then July 1st to:

Jun.-Prof. Dr. Simon Ebbinghaus
Physical Chemistry II (NCDF 03/352)
Ruhr-University Bochum
Universitätsstraße 150, 44801 Bochum
www.rub.de/pc2/ebbinghaus

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