• 1437867PublicAssets/3402
    Hsp33 Heat Shock Protein Inactive to Active
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    Hsp33 Heat Shock Protein Inactive to Active

    3402

    When the heat shock protein hsp33 is folded, it is inactive and contains a zinc ion, stabilizing the redox sensitive domain (orange). In the presence of an environmental stressor, the protein releases the zinc ion, which leads to the unfolding of the redox domain. This unfolding causes the chaperone to activate by reaching out its "arm" (green) to protect other proteins.
    Public Note
    Internal NoteIt's fine with me to put it in the media Gallery. Let me know if you need a better description.. All the best Dana Sent from my iPad On Sep 10, 2012, at 3:29 PM, "Toledo, Chelsea (NIH/NIGMS) [C]" wrote: Thank you so much, Dana! This looks great. Just to double-check, is it ok with you for this to go in our Media Gallery? It will appear with the description you gave below, as well as a credit to you, Ursula Jakob, and the University of Michigan. Thanks! Chelsea From: Dana Reichmann [mailto:danare@umich.edu] Sent: Saturday, September 08, 2012 6:37 PM To: Toledo, Chelsea (NIH/NIGMS) [C] Cc: Ursula Jakob Subject: Re: Time-sensitive: NIGMS image request Dear Chelsea, Please find the attached movie of Hsp33 in inactive (folded) and active (unfolded) states. Please let me know if you need me to make any corrections. thanks a lot Dana
    Keywords
    SourceDana Reichmann, University of Michigan
    Date2012-09-11 00:00:00
    Credit LineUrsula Jakob and Dana Reichmann, University of Michigan
    Investigator
    Record TypeVideo
    Topic Area(s);#Molecular Structures;#
    Previous Uses
    StatusActive

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3402_Hsp33_Heat_Shock_Protein_Inactive_to_Active_T.jpg
  
Thumbnail47 KB 3/28/2019 4:30 PMConstantinides, Stephen (NIH/NIGMS) [C]
Hsp33_Heat_Shock_Protein_Inactive_to_Active.mp4
  
High1405 KB 6/3/2016 3:28 PMaamishral2 (NIH/NIGMS) [C]

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