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Although allosteric transitions of GroEL by MgATP 2− have been widely studied, the initial bimolecular step of MgATP 2− binding to GroEL remains unclear. Here, we studied the equilibrium and kinetics of MgATP 2− binding to a variant of GroEL, in which Tyr485 was replaced by tryptophan, via isothermal titration calorimetry (ITC) and stopped-flow fluorescence spectroscopy...
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