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

ABSTRACT: 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.

SUBMITTER: Peris-Diaz MD

PROVIDER: S-EPMC10089061 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature

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

Peris-Díaz Manuel David MD Barkhanskiy Alexey A Liggett Ellen E Barran Perdita P Krężel Artur A

Chemical communications (Cambridge, England) 20230411 30

Ion mobility-mass spectrometry (IM-MS) unraveled different conformational stability in Zn<sub>4-7</sub>-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. ...[more]

PMID: 36960761

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