Ion mobility mass spectrometry and molecular dynamics simulations unravel the conformational stability of zinc metallothionein-2 species.
Manuel David Peris-DíazAlexey BarkhanskiyEllen LiggettPerdita E BarranArtur KrężelPublished in: Chemical communications (Cambridge, England) (2023)
Ion mobility-mass spectrometry (IM-MS) unraveled different conformational stability in Zn 4-7 -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 α-β domain interactions modulate protein unfolding.
Keyphrases
- molecular dynamics simulations
- mass spectrometry
- liquid chromatography
- molecular docking
- gas chromatography
- capillary electrophoresis
- heavy metals
- high performance liquid chromatography
- high resolution
- multiple sclerosis
- big data
- single cell
- ms ms
- tandem mass spectrometry
- binding protein
- risk assessment
- machine learning
- artificial intelligence
- single molecule
- simultaneous determination