离子淌度质谱和分子动力学模拟揭示锌金属硫蛋白-2 物种的构象稳定性。
Ion mobility mass spectrometry and molecular dynamics simulations unravel the conformational stability of zinc metallothionein-2 species.
机构信息
Department of Chemical Biology, Faculty of Biotechnology, University of Wrocław, F. Joliot-Curie 14a, 50-383 Wrocław, Poland.
Michael Barber Centre for Collaborative Mass Spectrometry, Manchester Institute of Biotechnology, 131 Princess Street, Manchester, M1 7DN, UK.
出版信息
Chem Commun (Camb). 2023 Apr 11;59(30):4471-4474. doi: 10.1039/d2cc06559b.
Ion mobility-mass spectrometry (IM-MS) unraveled different conformational stability in Zn-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.
离子淌度-质谱联用（IM-MS）揭示了锌金属硫蛋白-2 中的不同构象稳定性。我们引入了一种新的分子动力学模拟方法，该方法允许探索所有构象空间，证实了实验数据，并表明不仅 Zn-S 键，而且 α-β 结构域相互作用也调节蛋白质的展开。
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