XVIth International Workshop on
Quantum Systems in
Chemistry and Physics
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Structural analysis of ligand binding mechanism of Hsp90
Kazutomo Kawaguchi, Acep Purqon, Hiroaki Saito, Hidemi Nagao
Institute of Science and Engineering, Kanazawa University, Kanazawa 920-1192 Japan
Hsp90 is one of the molecular chaperones which protect their client proteins in the folding processes. Hsp90 usually forms a dimer and undergoes large conformational changes during its functional cycle. Binding and hydrolysis of ATP to ADP are required for these conformational changes. We performed molecular dynamics simulation of Hsp90 with ADP to elucidate molecular mechanisms of ligand binding process. The results of structural analysis of ligand binding process of Hsp90 will be presented and discussed through recent calculations.


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