Ion mobility mass spectrometry and molecular dynamics simulations unravel the conformational stability of zinc metallothionein-2 species

Ion mobility-mass spectrometry (IM-MS) unraveled different conformational stability in Zn4-7-metallothionein-2. We introduced a new molecular dynamics simulation approach that permitted the exploration of all of the conformational space confirming the experimental data, and revealed that not only the Zn-S bonds but also the alpha-beta domain interactions modulate protein unfolding.

Automated summary

Ion mobility-mass spectrometry (IM-MS) revealed different conformational stability in Zn4-7-metallothionein-2. A new molecular dynamics simulation approach was introduced, which explored all conformational space, confirmed experimental data, and revealed that both Zn-S bonds and alpha-beta domain interactions modulate protein unfolding.