User:Yash Patankar/Sandbox 1: Difference between revisions

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==Structures for Hsp90 homologs==
==Structures for Hsp90 homologs==
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Hsp90 is a ubiquitous protein and is conserved in many species. It shows a high amount of conservation in the N-terminal domain. Moreover, the active site, which is located in the N-terminal domain is highly conserved, which suggests a common mechanism for Hsp90. Also, there exists a dimerized state for HtpG, the bacterial homolog for Hsp90, and thus, there seems to be an ATPase coupled "molecular clamp" mechanism for Hsp90.