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Updated: May 13, 2026

Monitoring Protein-Ligand Interactions in Human Cells by Real-Time Quantitative In-Cell NMR using a High Cell Density Bioreactor
Published on: March 9, 2021
Atomic-resolution monitoring of protein maturation in live human cells by NMR
Lucia Banci1, Letizia Barbieri, Ivano Bertini
1CERM, Magnetic Resonance Center, University of Florence, Florence, Italy. banci@cerm.unifi.it
Abstract:
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.
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