Atomic-resolution monitoring of protein maturation in live human cells by NMR

Lucia Banci, Letizia Barbieri, Ivano Bertini, Enrico Luchinat, Erica Secci, Yuguang Zhao, Alexandru Aricescu

Research output: Contribution to journalArticlepeer-review


We use NMR directly in live human cells to describe the complete post-translational maturation process of human superoxide dismutase 1 (SOD1). We follow, at atomic resolution, zinc binding, homodimer formation and copper uptake, and discover that copper chaperone for SOD1 oxidizes the SOD1 intrasubunit disulfide bond through both copper-dependent and copper-independent mechanisms. Our approach represents a new strategy for structural investigation of endogenously expressed proteins in a physiological (cellular) environment.
Original languageEnglish
Pages (from-to)297-299
Number of pages3
JournalNature Chemical Biology
Issue number5
Publication statusPublished - May 2013


  • Cell Survival
  • Copper
  • HEK293 Cells
  • Humans
  • Nuclear Magnetic Resonance, Biomolecular
  • Oxidation-Reduction
  • Protein Conformation
  • Protein Processing, Post-Translational
  • Superoxide Dismutase
  • Zinc

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