Infos zum Job

The University Medical Center Göttingen is a tertiary care center and offers great de- velopment potential. Its 7,900 employees work in over 65 departments and facilities to provide top-quality patient care, excellent research and modern teaching. Göttingen,

"City of Science", located near the center of Germany, the University Medical Center

Göttingen is embedded in the city’s attractive network of scientific research facilities.

The University Medical Center Göttingen is a tertiary care center that offers great

development potential. Its 7,900 employees work in over 65 departments and facilities to provide top-quality patient care, excellent research and modern teaching. Situated in Göttingen, the "City of Science" located near the center of Germany, the University

Medical Center Göttingen is embedded in the city’s attractive network of scientific

research facilities.

The Core Facility Proteomics and the Cellular Biophysics and Translational Cardiology Section offer a research position for a highly motivated PhD student. The PhD project

"Mass spectrometric methods to study molecular nanodomain regulation of

cardiac ryanodine receptor function" is part of the Collaborative Research Center

(CRC) 1002, a competitive and highly interdisciplinary large-scale collaborative project (https://www.dfg.de/en/funded_projects/current_projects_programmes/list/projectdetail s/index.jsp?id=193793266&sort=nr_asc&prg=SFB).

Cardiomyocyte function depends on junctional nanodomains between the

sarcoendoplasmatic reticulum and the sarcolemma for localized control of Ca2+.

Clusters of the cardiac ryanodine receptor (RyR2) channel are at the core of Ca2+

release, and are tightly controlled by a complex set of highly specific protein/protein

interactions. The project goal is to develop and establish state-of-the-art proteomics

mass spectrometry approaches to elucidate the underlying mechanisms of action.

Building on established workflows, you will apply these approaches to cell culture,

animal model and human biopsy samples of defined cardiac disease models, and

complement your mass spectrometry work with protein biochemistry and

superresolution microscopy experiments. You will be located in the Core Facility

Proteomics and the Heart Research Center Göttingen, and participate campus-wide in CRC1002 and IRTG1816 activities. What you will be doing:

• Develop, apply and validate state-of-the-art quantitative mass spectrometrworkflows for global proteome profiling, protein/protein cross-linking, and analysis of posttranslational protein modifications in samples ranging from cell culture to human cardiac biopsies.
• Contribute your growing expertise to a range of cardiac research projectsacross the CRC1002 in a highly collaborative environment.
Who you are:

• A highly motivated candidate with a drive to learn and excel in science. You like to communicate with scientists and enjoy to work in an interdisciplinary, multicultural research environment.

Your background:

• Protein biochemistry, mass spectrometry, bioinformatics, cell and molecular biology.

Desirable training:

• Protein biochemistry (WB, pull-down), liquid chromatography-tandem mass spectrometry (LC/MS/MS), peptide and protein separations (SDS-PAGE, HPLC), statistical data analysis.
What our group offers:

• An exciting collaborative research environment with state-of-the-art massspectrometric methods and equipment at the University Medical Center.
• Our groups have jointly established advanced techniques in mass spectrometry- based proteomics. Our experience in methods teaching in interdisciplinaryteams will provide you with the knowledge and skills you need to carry out your experiments.
• A competitive scientific project embedded in a research center with plenty of opportunities to interact and learn from researchers from various disciplines.
• Scientific retreats and conferences are part of your work and provideopportunities for scientific networking and collaborations.
• Direct interaction with an active proteomics research community in Göttingen.

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