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Controlling biochemical pathways through chemically designed modulators may provide novel opportunities to develop therapeutic drugs and chemical tools. The underlying challenge is to design new molecular entities able to act as allosteric chemical switches that selectively turn on/off functions by modulating the conformational dynamics of their target protein. We examine the origins of the stimulation of ATPase and closure kinetics in the molecular chaperone Hsp90 by allosteric modulatorsdoi:10.1038/srep23830 pmid:27032695 pmcid:PMC4817115 fatcat:duidpjdxr5dxnjeyx7qihdew3i