Postdoctoral Researcher – Intrinsically Disordered Proteins

Big Science Sweden; Sweden; On-site; SEK 480,000 - 720,000; Full time

Job summary

Big Science Sweden is recruiting a Postdoctoral Researcher to lead a project on intrinsically disordered proteins at the European Spallation Source (ESS). The role involves advanced research using small-angle neutron scattering, method development, and computational modeling in collaboration with Lund University.

Ideal candidates will have a PhD in a related field and experience in relevant research techniques. Join us in pushing the frontiers of understanding protein behavior and function.

Qualifications

• PhD in relevant field (e.g., Computational Chemistry).
• Experience with small-angle neutron scattering techniques.
• Familiarity with programming and computational modeling.

Responsibilities

• Define and lead a research project on intrinsically disordered proteins.
• Develop advanced analysis strategies using machine learning.
• Collaborate with academic and research partners.

Job description

Postdoctoral Researcher – Intrinsically Disordered Proteins

Datum: 3 mars, 2026 Tid: 11:59

Placering: ESS

Mer information

ESS is looking for aPostdoctoral Researcher as part of the AMBER cofund project. This postdoctoral position will be based in the Large Scale Structures Division at the European Spallation Source (ESS) working with Dr. Andrew Jackson in collaboration with Prof. Marie Skepö at Lund University (Computational Chemistry).

The successful candidate will define and lead a project focused on intrinsically disordered proteins (IDPs) studied by small-angle neutron scattering. The work may explore self-assembling IDPs, both reversible and irreversible oligomer/aggregate formation, and should involve significant method development. A key component will be the development of advanced analysis strategies involving computational modelling (atomistic, coarse‑grained, hybrid, or multiscale approaches) and machine learning approaches to uncover the factors driving IDP behaviour and function.