An Integrated Mass Spectrometry and Molecular Dynamics Simulations Approach Reveals the Spatial Organization Impact of Metal-Binding Sites on the Stability of Metal-Depleted Metallothionein-2 Species
Manuel David Peris‐Díaz, Roman Guráň, Cármen Domene, Vivian de los Rı́os, Ondřej Zítka, Vojtěch Adam, Artur Krężel
Abstract
MT2 species and to explain the differences in binding affinities of Zn(II) ions to MTs. Differences are found to be the result of the degree of water participation in MT (un)folding and the hyper-reactive character of Cys21 and Cys29 residues. The thermodynamics properties of Zn(II) (un)binding to MT2 are found to differ from those of Cd(II), justifying their distinctive roles. The potential of this integrated strategy in the investigation of numerous unexplored metalloproteins is attested by the results highlighted in the present study.
Topics & Concepts
ChemistryMetallothioneinAffinitiesMolecular dynamicsMetalMetal ions in aqueous solutionMetadynamicsMass spectrometryPhytochelatinZincBinding affinitiesIonCrystallographyBiophysicsComputational chemistryStereochemistryBiochemistryChromatographyReceptorEnzymeBiologyOrganic chemistryGlutathioneTrace Elements in HealthIron Metabolism and DisordersPlant Micronutrient Interactions and Effects