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 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...

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Detalles Bibliográficos
Autores principales: Peris-Díaz, Manuel David, Barkhanskiy, Alexey, Liggett, Ellen, Barran, Perdita, Krężel, Artur
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Royal Society of Chemistry 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10089061/
https://www.ncbi.nlm.nih.gov/pubmed/36960761
http://dx.doi.org/10.1039/d2cc06559b
Descripción
Sumario: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.