Zinc ions bridging two ubiquitin molecules (with His68 at the interface) contribute to select a subset of conformers from the noncovalent dimer ensemble, thus restricting quaternary structure dynamics, which hampers apo-protein crystallization. The type of selected conformer is shown to determine the crystal packing which varies from orthorhombic to cubic symmetry
S. Fermani, G. Falini, M. Calvaresi, A. Bottoni, V. Calò, V. Mangini, et al. (2013). Conformational Selection of Ubiquitin Quaternary Structures Driven by Zinc Ions. CHEMISTRY-A EUROPEAN JOURNAL, 19(46), 15480-15484 [10.1002/chem.201302229].
Conformational Selection of Ubiquitin Quaternary Structures Driven by Zinc Ions
FERMANI, SIMONA;FALINI, GIUSEPPE;CALVARESI, MATTEO;BOTTONI, ANDREA;
2013
Abstract
Zinc ions bridging two ubiquitin molecules (with His68 at the interface) contribute to select a subset of conformers from the noncovalent dimer ensemble, thus restricting quaternary structure dynamics, which hampers apo-protein crystallization. The type of selected conformer is shown to determine the crystal packing which varies from orthorhombic to cubic symmetryFile in questo prodotto:
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