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Heat-shock protein 90 (Hsp90) promotes the maturation and stability of its client proteins, including many kinases. In doing so, Hsp90 may allow its clients to accumulate mutations as previously proposed by the capacitor hypothesis. If true, Hsp90 clients should show increased evolutionary rate compared to non-clients; however, other factors, such as gene expression and protein connectivity, may confound or obscure the chaperone's putative contribution. Here, we compared the evolutionary ratesdoi:10.1101/006411 fatcat:k22zclxlx5h4rixsrf2i6iumhe