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

Protein Expression and Purification 2026 Open access

Read full text
Authors: Minsu Kim, Joonhyeok Choi, Hae-Kap Cheong, Kyoung‐Seok Ryu, Jin-Wan Park, Jung-Hye Ha, Jong-Soo Lim, Woo Sung Son, Sangwook Wu, Donghan Lee
DOI: 10.1016/j.pep.2026.106940
Cited by: 1
References: 29

Abstract

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.

Fields of Study & Subjects

Nuclear Structure and Function Sirtuins and Resveratrol in Medicine Heat shock proteins research

Publication details

Journal / source
Protein Expression and Purification
Publisher
Elsevier BV
Volume
242
Pages
106940–106940
Publication date
4 May 2026
Language
EN