Offer Description
Project Title: Unravelling the role of posttranslational modifications (PTMs) in β-catenin interactions
Objectives:
- Generate semi-synthetic β-catenin IDR variants bearing site-specific PTMs.
- Characterize the conformational properties and interactions of disordered segments of β-catenin.
- Elucidate which PTMs are critical for β-catenin interactions and regulation.
Project Overview: Efforts to develop therapeutic molecules targeting β-catenin and structural biology studies of its interactions have focused mainly on the structured domains of β-catenin. However, the intrinsically disordered N- and C-terminal domains are key sites for β-catenin regulation and interactions, many of which are fine-tuned by posttranslational modifications (PTMs). The aim of this project is to use protein chemistry techniques to generate site-specifically modified variants of β-catenin, focusing on the N-terminal domain, which is a regulatory region for the binding of various interaction partners, e.g., regulating the degradation of β-catenin. This project builds on expertise for protein synthesis, ligation, and modification in the Conibear group and utilizes expertise in structural biology of intrinsically-disordered regions (Madl group) and protein expression (Grossmann group) to elucidate the role of PTMs in β-catenin regulation. The innovation in this project is the ability to unravel effects of site-specific posttranslational modifications of β-catenin, individually and in combination, which would be extremely difficult using other techniques. Structural and functional characterization of the modified variants has the potential to uncover new sites and interaction partners for therapeutic intervention.
Contribution to the overall research program: Providing unique access to site-specifically modified β-catenin N-terminal variants for structure and binding studies.
Skills and research profile:
- Completion of a master or diploma curriculum in chemistry or chemical biology, or closely related field. Ability to carry out laboratory experimental work and data analysis skilfully and responsibly.
- Interest in research in the field of protein chemistry: Curiosity, self-motivation, resilience, and willingness to learn.
- Experience in one or more of the following scientific fields: Peptide synthesis and characterisation, NMR spectroscopy of peptides/proteins, protein expression and purification.
- Enthusiasm for scientific communication and public engagement.
- Teamwork, innovation and problem-solving skills.
Salary: The position is funded by the Horizon Europe MSCA-DN project FlexCAT (Grant Agreement No. 101311592) for three years. The selected candidate will be offered a competitive salary comprising a Living Allowance (adjusted by the country correction coefficient), a Mobility Allowance, and, if applicable, a Family Allowance. All allowances are subject to applicable social security contributions and taxation.
Planned secondment: 1. Host: University of Göttingen; Supervisor: Prof. Tom Grossmann; Length: 3 months. Purpose: Structural and binding characterization of site-specifically modified β-catenin variants using X-ray crystallography and binding assays. Enrolment in Doctoral degree(s): TU Wien, Faculty of Technical Chemistry (Conibear)
How to apply: Applications are exclusively accepted through the Recruitment Portal (https://phd-recruiting.medunigraz.at/).
The required information is specified in the recruitment portal and comprises:
- Motivation statement for selected DC projects
- Detailed CV; publication list if applicable
- BSc/MSc diplomas and academic transcripts/supplements
- Contact details for two referees
Applications will be assessed for eligibility and scientific/academic quality. Shortlisted applicants will be invited to interview. The final selection will follow the open, transparent and merit-based recruitment principles of MSCA.
Key dates:
- Applications open: 15 September 2026
- Applications close: 31 October 2026
- Online pre-interviews: early November 2026
- Final interviews: late November/early December 2026
- Decisions and offers: mid-December 2026
- Start: January 2027 – March 2027
Data protection statement
The personal data you provide as part of your application will be processed for the purposes necessary to administer the recruitment and selection process for the Doctoral Candidate position(s) for which you apply within the FlexCAT Marie Skłodowska-Curie Doctoral Network (MSCA-DN). Access to your application will be restricted to individuals directly involved in the recruitment and selection process, including the recruiting beneficiary, members of the selection committee, and, where necessary, authorised representatives of the FlexCAT consortium. Personal data will be processed in accordance with the applicable data-protection legislation, including the General Data Protection Regulation (EU) 2016/679 (GDPR), and the privacy policies of the recruiting beneficiary. Statistics for project reporting will be provided in anonymised or appropriately aggregated form.
Requirements
Research Field: Chemistry
Education Level: Master Degree or equivalent
Skills/Qualifications:
Applicants of any nationality are welcome to apply. To be eligible for recruitment as an MSCA Doctoral Candidate, applicants must fulfil the following criteria at the date of recruitment:
- Education – you do not hold a doctoral degree and hold (or will shortly complete) a science Master's degree (see individual project requirements), with excellent results, qualifying you for admission to the doctoral program of the respective host institution. The successful candidate must fulfil the admission requirements of the respective doctoral programme and will be enrolled in a doctoral programme during the project.
- Mobility - you must not have resided or carried out your main activity (work, studies, etc.) in recruiting beneficiary's country for more than 12 months during the 36 months before your recruitment. Compulsory national service, holidays/short stays and time spent obtaining refugee status under the Geneva Convention4 are not considered for this purpose.
- Language & communication – excellent command of spoken and written English (min. B2 level). Ability to communicate results clearly to diverse audiences, both in writing and verbally.
- Motivation – motivation for multidisciplinary, international doctoral research, hands-on experimental work, mandatory academic/industy secondment(s), to publish research findings in international journals, present results at conferences and contribute to project deliverables. Willingness to contribute to project network-wide activities, communication, training events, and dissemination efforts.
- Technical skills – specific to the individual DC project (see individual project descriptions).
Specific Requirements:
Skills and research profile:
- Completion of a master or diploma curriculum in chemistry or chemical biology, or closely related field. Ability to carry out laboratory experimental work and data analysis skilfully and responsibly.
- Interest in research in the field of protein chemistry: Curiosity, self-motivation, resilience, and willingness to learn.
- Experience in one or more of the following scientific fields: Peptide synthesis and characterisation, NMR spectroscopy of peptides/proteins, protein expression and purification.
- Enthusiasm for scientific communication and public engagement.
- Teamwork, innovation and problem-solving skills.
Languages: ENGLISH
Level: Excellent
Research Field: Chemistry
Years of Research Experience: 1 - 4

