Enhanced large-scale production and purification of recombinant human NUPR1 for detailed structural and functional insights

C were successfully implemented, enabling detailed multi-dimensional NMR spectroscopic analysis. Preliminary NMR data, including backbone resonance assignments, unequivocally confirmed the intrinsically disordered nature of NUPR1. Secondary structure propensity analysis derived from these assignments indicated a characteristically low propensity for the formation of stable canonical secondary structures. This robust, well-characterized, and scalable expression and purification pipeline provides an essential and solid foundation for future detailed structural, dynamic, and functional investigations of NUPR1, which are crucial for dissecting its complex roles in cellular physiology and disease pathogenesis.