Hsp90 is a molecular chaperone which has been shown to be ATP-dependent in vivo. The present thesis comprises a detailled kinetic analysis of the individual steps of the ATPase cycle of Hsp90 from S. cerevisiae. The analysis led to the identification of a molecular rearrangement within the Hsp90 molecule, which results in a determination of the bound nucleotide for hydrolysis. Furthermore, specific functions of the Hsp90 partner protein p23 were mapped to defined structural domains of the p23 molecule.
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Hsp90 is a molecular chaperone which has been shown to be ATP-dependent in vivo. The present thesis comprises a detailled kinetic analysis of the individual steps of the ATPase cycle of Hsp90 from S. cerevisiae. The analysis led to the identification of a molecular rearrangement within the Hsp90 molecule, which results in a determination of the bound nucleotide for hydrolysis. Furthermore, specific functions of the Hsp90 partner protein p23 were mapped to defined structural domains of the p23 mo...
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