A technique that can track proteins at atomic resolution in live cells could help to show how proteins fold and mature into functional forms.

A protein's environment strongly influences its maturation, but most analyses of protein dynamics require purified components. Radu Aricescu of the University of Oxford, UK, Lucia Banci of the University of Florence, Italy, and their groups used nuclear magnetic resonance spectroscopy to track the structure of the protein SOD1 in human cells.

The technique showed that another protein helps SOD1 to bind zinc and copper, and form internal disulphide bonds that aid stability. The method also showed that disulphide bonds can form even when SOD1 has not bound copper, a result that has not been seen using purified proteins.

Nature Chem. Biol. http://dx.doi.org/10.1038/nchembio.1202 (2013)